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Conserved domains on  [gi|2462537201|ref|XP_054230564|]
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propionyl-CoA carboxylase alpha chain, mitochondrial isoform X18 [Homo sapiens]

Protein Classification

acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha( domain architecture ID 11469138)

acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha is a biotin-dependent carboxylase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
63-358 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 549.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:COG4770    82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:COG4770   162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:COG4770   242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEH 297
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
63-358 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 549.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:COG4770    82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:COG4770   162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:COG4770   242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEH 297
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 62-358 3.26e-169

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 479.30  E-value: 3.26e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  62 TFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHP 141
Cdd:PRK08591    1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 142 GYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAS 221
Cdd:PRK08591   81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 222 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 301
Cdd:PRK08591  161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462537201 302 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:PRK08591  241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEH 297
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 63-360 1.04e-140

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 407.22  E-value: 1.04e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPV 299
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 176-358 3.85e-86

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 259.16  E-value: 3.85e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 176 DKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGD 255
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 256 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTV 335
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160

                         170       180
                  ....*....|....*....|....
gi 2462537201 336 EFLVDSK-KNFYFLEMNTRLQVLH 358
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEH 184
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
63-358 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 549.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:COG4770    82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:COG4770   162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:COG4770   242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEH 297
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 62-358 3.26e-169

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 479.30  E-value: 3.26e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  62 TFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHP 141
Cdd:PRK08591    1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 142 GYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAS 221
Cdd:PRK08591   81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 222 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 301
Cdd:PRK08591  161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462537201 302 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:PRK08591  241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEH 297
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 63-358 1.42e-162

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 462.58  E-value: 1.42e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK06111    2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK06111   82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK06111  162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:PRK06111  242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEH 297
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
63-360 2.08e-151

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 435.95  E-value: 2.08e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK08654    2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK08654   82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK08654  162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVdSKKNFYFLEMNTRLQVLHII 360
Cdd:PRK08654  242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPI 298
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
63-360 1.31e-142

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 411.80  E-value: 1.31e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK05586    2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK05586   82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK05586  162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:PRK05586  242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPI 299
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 63-360 1.04e-140

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 407.22  E-value: 1.04e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPV 299
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 61-360 7.85e-137

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 417.56  E-value: 7.85e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201   61 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPA--PTsKSYLNMDAIMEAIKKTRAQA 138
Cdd:COG1038      2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGkgPV-DAYLDIEEIIRVAKEKGVDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  139 VHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMI 218
Cdd:COG1038     81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  219 KASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQK 298
Cdd:COG1038    161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462537201  299 VVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:COG1038    241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTV 302
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 60-360 6.97e-134

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 409.91  E-value: 6.97e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201   60 EKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVG--PAPtSKSYLNMDAIMEAIKKTRAQ 137
Cdd:PRK12999     2 MKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGegKHP-VRAYLDIDEIIRVAKQAGVD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  138 AVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVM 217
Cdd:PRK12999    81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  218 IKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQ 297
Cdd:PRK12999   161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462537201  298 KVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:PRK12999   241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTV 303
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
65-360 1.74e-122

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 360.60  E-value: 1.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  65 KILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYG 144
Cdd:PRK08462    6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 145 FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGG 224
Cdd:PRK08462   86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 225 GGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAP 304
Cdd:PRK08462  166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462537201 305 SIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:PRK08462  246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTV 301
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 61-358 4.91e-119

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 352.52  E-value: 4.91e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  61 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVH 140
Cdd:PRK12833    3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 141 PGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKA 220
Cdd:PRK12833   83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 221 SAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHgNALWLNERECSIQRRNQKVV 300
Cdd:PRK12833  163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462537201 301 EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVLH 358
Cdd:PRK12833  242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEH 300
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
63-360 6.16e-119

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 352.48  E-value: 6.16e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSkSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK07178    2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK07178   81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK07178  161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLHII 360
Cdd:PRK07178  241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTI 298
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 63-358 1.11e-106

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 321.38  E-value: 1.11e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTsKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK08463    2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRI-AREIGYPVMIKAS 221
Cdd:PRK08463   81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 222 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 301
Cdd:PRK08463  161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462537201 302 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVLH 358
Cdd:PRK08463  241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEH 297
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 176-358 3.85e-86

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 259.16  E-value: 3.85e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 176 DKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGD 255
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 256 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTV 335
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160

                         170       180
                  ....*....|....*....|....
gi 2462537201 336 EFLVDSK-KNFYFLEMNTRLQVLH 358
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEH 184
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 63-170 2.94e-63

Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.


Pssm-ID: 425585 [Multi-domain]  Cd Length: 108  Bit Score: 196.94  E-value: 2.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 2462537201 143 YGFLSENKEFARCLAAEDVVFIGPDTHA 170
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 123-359 4.32e-49

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 165.82  E-value: 4.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 123 NMDAIMEAIKKTRAQavHPGYGFLSENkEFARCLAAEdVV----FIGPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgV 198
Cdd:COG0439     1 DIDAIIAAAAELARE--TGIDAVLSES-EFAVETAAE-LAeelgLPGPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 199 VKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDk 278
Cdd:COG0439    75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 279 HGNALWlnereCSIQRRNQK---VVE---EAPSIfLDAETRRAMGEQAVALARAVKYS-SAGTVEFLVDSKKNFYFLEMN 351
Cdd:COG0439   153 DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEIN 226


                  ....*...
gi 2462537201 352 TRLQVLHI 359
Cdd:COG0439   227 ARLGGEHI 234
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 75-353 5.33e-18

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 85.32  E-value: 5.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  75 ACRVIRtckKMGIKTVAIHS-------DVDassvhvkMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG--- 144
Cdd:COG0458    21 ACKALR---EEGYEVILVNSnpetvstDYD-------TAD-RLYFEP-------LTVEDVLDIIEKEKPDGVIVQFGgqt 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 145 ------FLSENKEFarclaaEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIG 213
Cdd:COG0458    83 alnlavELEEAGIL------EGVKILGTSPDAI----DLAEdrelfKELL-DKLGIPQPKS--GTATSVEEALAIAEEIG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 214 YPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSsqeaassfGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnere 289
Cdd:COG0458   150 YPVIVRPSYVLGGRGMGIVYNEEEleeyLERALKVS--------PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV---- 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462537201 290 CSIQrrNqkvVEEA-----------PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 353
Cdd:COG0458   218 GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 126-352 1.20e-13

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 70.52  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 126 AIMEAIKKTRAQAVhpgyGFLSENKEFARCLAAE--DVVFI--------------------------GPDTHAIqAMgDK 177
Cdd:COG1181    23 AVAAALDKAGYDVV----PIGIDVEDLPAALKELkpDVVFPalhgrggedgtiqgllellgipytgsGVLASAL-AM-DK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 178 IESKLLAKKAEVNTIPGFdgVVKDAEEAV--RIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgD 255
Cdd:COG1181    97 ALTKRVLAAAGLPTPPYV--VLRRGELADleAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAAL-----EEAFKY-D 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 256 DRLLIEKFIDnPRHIEIQVLGDKHGNALWLNErecsIQRRN-----------QKVVEEAPSIfLDAETRRAMGEQAVALA 324
Cdd:COG1181   169 DKVLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEELEERIQELALKAF 242

                         250       260
                  ....*....|....*....|....*...
gi 2462537201 325 RAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:COG1181   243 RALGCRGYARVDFRLDEDGEPYLLEVNT 270
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 78-353 2.10e-12

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 68.49  E-value: 2.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201   78 VIRTCKKMGIKTVAIHSDVDASSVHVKMADeavcvgpaptsKSY---LNMDAIMEAIKKTRAQAVHPGYGFLSENKeFAR 154
Cdd:TIGR01369  580 AVLALRELGYETIMINYNPETVSTDYDTSD-----------RLYfepLTFEDVMNIIELEKPEGVIVQFGGQTPLN-LAK 647

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  155 CLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGM 229
Cdd:TIGR01369  648 ALEEAGVPILGTSPESI----DRAEdrekfSELL-DELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  230 RIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPRHIEIQVLGDkHGNALwlnerECSIQRRnqkvVEEA------ 303
Cdd:TIGR01369  721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVL-----IPGIMEH----IEEAgvhsgd 786

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462537201  304 -----PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTR 353
Cdd:TIGR01369  787 stcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPR 840
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 173-352 2.80e-12

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 66.67  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 173 AMgDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEaass 252
Cdd:PRK01372   96 AM-DKLRTKLVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKY---- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 253 fgDDRLLIEKFIDNPrhiEIQ--VLGDKhgnALwlnerecsiqrrnqKVVE-EAPSIF-------------------LDA 310
Cdd:PRK01372  169 --DDEVLVEKYIKGR---ELTvaVLGGK---AL--------------PVIEiVPAGEFydyeakylaggtqyicpagLPA 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462537201 311 ETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:PRK01372  227 EIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
78-354 2.94e-12

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 67.26  E-value: 2.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  78 VIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVcVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGY----GFLSENKEFA 153
Cdd:COG3919    20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVV-VVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 154 rclaAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKASaggggkgMRIAW 233
Cdd:COG3919    99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPA-------DSVGY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 234 DD---EETRDGFRLSSQEA------ASSFGDDRLLIEKFIDNPRHIEIQVLG--DKHGNALWLnereCSIQRRNQKVVEE 302
Cdd:COG3919   166 DElsfPGKKKVFYVDDREEllallrRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAG 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462537201 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRL 354
Cdd:COG3919   242 GNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRF 294
carB PRK05294
carbamoyl-phosphate synthase large subunit;
153-274 1.72e-09

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 59.34  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  153 ARCLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKAS------ 221
Cdd:PRK05294   646 AKALEAAGVPILGTSPDAI----DLAEdrerfSKLL-EKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSyvlggr 718

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462537201  222 AggggkgMRIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPrhIEIQV 274
Cdd:PRK05294   719 A------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGA--IEVDV 759
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 58-354 9.75e-09

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 56.93  E-value: 9.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201   58 PNEKTFDKILVANRGEI----AC-------RVIRTCKKMGIKTVAIHSDVDASSVHVKMADEaVCVGPaptsksyLNMDA 126
Cdd:TIGR01369    1 PKRTDIKKILVIGSGPIvigqAAefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADK-VYIEP-------LTPEA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  127 IMEAIKKTRAQAVHPGYG-----FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKD 201
Cdd:TIGR01369   73 VEKIIEKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESE--IAHS 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  202 AEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSSQeaassfgdDRLLIEKFIDNPRHIEIQVLGD 277
Cdd:TIGR01369  151 VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREElkeiAERALSASPI--------NQVLVEKSLAGWKEIEYEVMRD 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  278 KHGNALWLnereCSIQrrN----------QKVVeeAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSK-KNFY 346
Cdd:TIGR01369  223 SNDNCITV----CNME--NfdpmgvhtgdSIVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYY 294


                   ....*...
gi 2462537201  347 FLEMNTRL 354
Cdd:TIGR01369  295 VIEVNPRV 302
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 164-353 6.18e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 54.59  E-value: 6.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  164 IGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEEtrdgfr 243
Cdd:PRK12815   658 LGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA------ 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  244 LSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDkhGNALWLN---ERecsiqrrnqkvVEEA-----------PSIFLD 309
Cdd:PRK12815   730 LEAYLAENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiEH-----------IEQAgvhsgdsiavlPPQSLS 795

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462537201  310 AETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTR 353
Cdd:PRK12815   796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNPR 838
ddl PRK01966
D-alanine--D-alanine ligase;
163-352 5.38e-07

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 50.89  E-value: 5.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 163 FIGPDTHAiQAMG-DKIESKLLAKKAEVNTIPGfdgVV---KDAEEAV--RIAREIGYPVMIKASaggggkgmriawdde 236
Cdd:PRK01966  110 YVGCGVLA-SALSmDKILTKRLLAAAGIPVAPY---VVltrGDWEEASlaEIEAKLGLPVFVKPA--------------- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 237 etRDGfrlssqeaaSSFG--------------------DDRLLIEKFIdNPRHIEIQVLGdkhgnalwlNERECSiqrrn 296
Cdd:PRK01966  171 --NLG---------SSVGiskvkneeelaaaldlafeyDRKVLVEQGI-KGREIECAVLG---------NDPKAS----- 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462537201 297 qkVVEE--APSIFLD-------------------AETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:PRK01966  225 --VPGEivKPDDFYDyeakyldgsaeliipadlsEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
PLN02735 PLN02735
carbamoyl-phosphate synthase
 166-281 7.50e-07

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 51.32  E-value: 7.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  166 PDThaIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRdgfrlS 245
Cdd:PLN02735   694 PDS--IDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK-----T 764

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462537201  246 SQEAASSFGDDR-LLIEKFIDNPRHIEIQVLGDKHGN 281
Cdd:PLN02735   765 YLETAVEVDPERpVLVDKYLSDATEIDVDALADSEGN 801
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 105-353 2.43e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 48.73  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 105 MADEAVcVGPAPTSKSYLnmDAIMEAIKKTRAQAVHPGY----GFLSENKEFarcLAAEDVVFIGPDTHAIQAMGDKIES 180
Cdd:PRK12767   42 FADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRDR---FEEIGVKVLVSSKEVIEICNDKWLT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 181 KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG------FRLSSQEAASSFG 254
Cdd:PRK12767  116 YEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKP------------------RDGsasigvFKVNDKEELEFLL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 255 DDR--LLIEKFIDNPRhIEIQVLGDKHGNALwlnereCSIQRR---------NQKVVEEAPSIFldaetrramgEQAVAL 323
Cdd:PRK12767  178 EYVpnLIIQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKrievragetSKGVTVKDPELF----------KLAERL 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 2462537201 324 ARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 353
Cdd:PRK12767  241 AEALGARGPLNIQCFVTDGE-PYLFEINPR 269
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 156-354 2.52e-06

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 49.58  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  156 LAAEDVVFIGPDTHAIQAMGDKIESKLLAKKaevNTIP-GFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWD 234
Cdd:PRK12815   108 LEQYGVELLGTNIEAIQKGEDRERFRALMKE---LGEPvPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAEN 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  235 DEETRDGFRlsSQEAASSFGDdrLLIEKFIDNPRHIEIQVLGDKHGNALWLNERE----CSIQRRNQKVVeeAPSIFL-D 309
Cdd:PRK12815   185 LEELEQLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVCNMEnidpVGIHTGDSIVV--APSQTLtD 258

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462537201  310 AETRRaMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRL 354
Cdd:PRK12815   259 DEYQM-LRSASLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRV 303
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 211-352 2.56e-06

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 47.70  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 211 EIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgDDRLLIEKFIDNpRHIEIQVLGDKHGNALWLNER-- 288
Cdd:pfam07478  34 ALGYPVFVKPARLGSSVGVSKVESREELQAAI-----EEAFQY-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvp 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462537201 289 ECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALA----RAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:pfam07478 107 SGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELAlkayKALGCRGLARVDFFLTEDGEIVLNEVNT 174
carB PRK05294
carbamoyl-phosphate synthase large subunit;
75-282 2.01e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 46.63  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201   75 ACRVIRtckKMGIKTVAIHSDV-----DAssvhvKMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG----- 144
Cdd:PRK05294    33 ACKALR---EEGYRVVLVNSNPatimtDP-----EMAD-ATYIEP-------ITPEFVEKIIEKERPDAILPTMGgqtal 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  145 ----FLSENKEFARClaaeDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIka 220
Cdd:PRK05294    97 nlavELAESGVLEKY----GVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVII-- 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462537201  221 saggggkgmR-----------IAWDDEETRD----GFRLS--SQeaassfgddrLLIEKFIDNPRHIEIQVLGDKHGNA 282
Cdd:PRK05294   169 ---------RpsftlggtgggIAYNEEELEEiverGLDLSpvTE----------VLIEESLLGWKEYEYEVMRDKNDNC 228
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 83-265 1.10e-04

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 43.52  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  83 KKMGIKTVAIHSDVDASSVHVkmADEAVcVGPaptsksYLNMDAIMEAIKktRAQAVhpgyGFLSEN--KEFARCLAAED 160
Cdd:COG0026    11 KRLGYRVHVLDPDPDSPAAQV--ADEHI-VAD------YDDEEALREFAE--RCDVV----TFEFENvpAEALEALEAEV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 161 VVFigPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeeTRD 240
Cdd:COG0026    76 PVR--PGPEALEIAQDRLLEKAFLAELGIPV-APFA-AVDSLEDLEAAIAELGLPAVLKT-----------------RRG 134

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462537201 241 G------FRLSSQE----AASSFGDDRLLIEKFID 265
Cdd:COG0026   135 GydgkgqVVIKSAAdleaAWAALGGGPCILEEFVP 169
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 83-265 3.36e-04

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 42.06  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  83 KKMGIKTVAIhsDVDASSVHVKMADEAVCVgpaptskSYLNMDAIMEAIKktRAQAVhpGYGFlsEN--KEFARCLAAED 160
Cdd:PRK06019   22 APLGYKVIVL--DPDPDSPAAQVADEVIVA-------DYDDVAALRELAE--QCDVI--TYEF--ENvpAEALDALAARV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 161 VVFIGPDthAIQAMGDKIESKLLAKKAEVNTiPGFdGVVKDAEEAVRIAREIGYPVMIKasaggggkgmriawddeeTR- 239
Cdd:PRK06019   87 PVPPGPD--ALAIAQDRLTEKQFLDKLGIPV-APF-AVVDSAEDLEAALADLGLPAVLK------------------TRr 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462537201 240 ---DG---FRLSS----QEAASSFGDDRLLIEKFID 265
Cdd:PRK06019  145 ggyDGkgqWVIRSaedlEAAWALLGSVPCILEEFVP 180
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
179-220 3.49e-04

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 42.42  E-value: 3.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462537201 179 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKA 220
Cdd:COG1042   492 EAKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 179-219 7.44e-04

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 463918 [Multi-domain]  Cd Length: 221  Bit Score: 40.54  E-value: 7.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462537201 179 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIK 219
Cdd:pfam13549  14 EAKALLAAYGIPVVPT--RLARSPEEAVAAAEEIGYPVVLK 52
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 197-264 1.23e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 40.91  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 197 GVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG-------FRLSSQE-------AASSFGDDrLLIEK 262
Cdd:PRK14016  233 RVVTSAEDAWEAAEEIGYPVVVKP------------------LDGnhgrgvtVNITTREeieaayaVASKESSD-VIVER 293


                  ..
gi 2462537201 263 FI 264
Cdd:PRK14016  294 YI 295
PLN02735 PLN02735
carbamoyl-phosphate synthase
 129-354 3.78e-03

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 39.38  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  129 EAIKKTRAQAVHPGYG---FLSENKEFAR--CLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPgfDGVVKDAE 203
Cdd:PLN02735    92 QVIAKERPDALLPTMGgqtALNLAVALAEsgILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLD 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  204 EAVRIAREIG-YPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSfgddRLLIEKFIDNPRHIEIQVLGDKHGNA 282
Cdd:PLN02735   170 ECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELEVMRDLADNV 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201  283 LWLnereCSIQRRNQKVVEEAPSI-------FLDAETRRaMGEQAVALARAVKYSSAGT-VEFLVDSKK-NFYFLEMNTR 353
Cdd:PLN02735   246 VII----CSIENIDPMGVHTGDSItvapaqtLTDKEYQR-LRDYSVAIIREIGVECGGSnVQFAVNPVDgEVMIIEMNPR 320


                   .
gi 2462537201  354 L 354
Cdd:PLN02735   321 V 321
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 152-351 4.25e-03

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 38.38  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 152 FARCLAAEDVVFIgPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKasaggggkgmri 231
Cdd:COG0189    73 LLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVLK------------ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537201 232 awddeeTRDG------FRLSSQEAASSF-------GDDRLLIEKFIDNPRHIEIQ--VLGDKHGNALW--LNERECSIQR 294
Cdd:COG0189   138 ------PLDGsggrgvFLVEDEDALESIlealtelGSEPVLVQEFIPEEDGRDIRvlVVGGEPVAAIRriPAEGEFRTNL 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462537201 295 RNQKVVEEAPsifLDAETRramgEQAVALARAVKYSSAGtVEFLVDsKKNFYFLEMN 351
Cdd:COG0189   212 ARGGRAEPVE---LTDEER----ELALRAAPALGLDFAG-VDLIED-DDGPLVLEVN 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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