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Conserved domains on  [gi|767978886|ref|XP_011519395|]
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propionyl-CoA carboxylase alpha chain, mitochondrial isoform X4 [Homo sapiens]

Protein Classification

biotin carboxylase domain-containing protein( domain architecture ID 1903193)

biotin carboxylase domain-containing protein similar to Blastocladiella emersonii acetyl-coenzyme-A carboxylase converts acetyl-CoA to malonyl-CoA, which is converted to malonyl-acyl carrier protein (ACP), the building block of the fatty acid moieties of bacterial membrane lipids

PubMed:  31023230

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];
63-512 0e+00

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


:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 808.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:COG4770    2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:COG4770   82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:COG4770  162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:COG4770  242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:COG4770  322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 767978886 463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 512
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
525-633 1.88e-25

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


:

Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 101.94  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  525 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 604
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
                          90       100
                  ....*....|....*....|....*....
gi 767978886  605 VSVDGTQRTVQClSREAGGnMSIQFLGTV 633
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTS 106
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
63-512 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 808.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:COG4770    2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:COG4770   82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:COG4770  162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:COG4770  242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:COG4770  322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 767978886 463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 512
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
62-504 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 682.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  62 TFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHP 141
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 142 GYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAS 221
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 222 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 301
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 302 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 381
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 382 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSD 458
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGET 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 767978886 459 RTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
63-504 0e+00

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: 575.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 767978886  463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
176-383 2.78e-102

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: 311.55  E-value: 2.78e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  176 DKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGD 255
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  256 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTV 335
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767978886  336 EFLVDSK-KNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLR 383
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
397-504 1.18e-49

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 168.75  E-value: 1.18e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   397 ECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 476
Cdd:smart00878   1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78
                           90       100
                   ....*....|....*....|....*...
gi 767978886   477 GVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:smart00878  79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
525-633 1.88e-25

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 101.94  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  525 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 604
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
                          90       100
                  ....*....|....*....|....*....
gi 767978886  605 VSVDGTQRTVQClSREAGGnMSIQFLGTV 633
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTS 106
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
63-512 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 808.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:COG4770    2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:COG4770   82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:COG4770  162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:COG4770  242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:COG4770  322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 767978886 463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 512
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
62-504 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 682.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  62 TFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHP 141
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 142 GYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAS 221
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 222 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 301
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 302 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 381
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 382 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSD 458
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGET 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 767978886 459 RTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
63-522 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 654.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK06111   2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK06111  82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPyKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTF-FPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDvypdgfkgHMLTKSEK 522
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK--------QLVKKSTK 450
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
63-506 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 634.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK08654   2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK08654  82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVdSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDF-APSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 767978886 463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 506
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
63-504 0e+00

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: 575.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 767978886  463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
63-506 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 573.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK05586   2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK05586  82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQyqepLHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDR 459
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGF-MPCPGKIEE----LYIPGglgVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDR 396
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 767978886 460 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 506
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
60-506 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 571.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   60 EKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVG--PAPtSKSYLNMDAIMEAIKKTRAQ 137
Cdd:PRK12999    2 MKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGegKHP-VRAYLDIDEIIRVAKQAGVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  138 AVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVM 217
Cdd:PRK12999   81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  218 IKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQ 297
Cdd:PRK12999  161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  298 KVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVA 377
Cdd:PRK12999  241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  378 KGYPLR------HKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQ-PGSDISIYYDPMIS 450
Cdd:PRK12999  321 EGATLHdleigiPSQEDIRLRGYAIQCRITTEDPANNF-MPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLLV 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767978886  451 KLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 506
Cdd:PRK12999  399 KLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
61-503 0e+00

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: 561.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   61 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPA--PTsKSYLNMDAIMEAIKKTRAQA 138
Cdd:COG1038     2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGkgPV-DAYLDIEEIIRVAKEKGVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  139 VHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMI 218
Cdd:COG1038    81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  219 KASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQK 298
Cdd:COG1038   161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  299 VVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAK 378
Cdd:COG1038   241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  379 GYPLRHK------QADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSG-IQPGSDISIYYDPMISK 451
Cdd:COG1038   321 GYSLDDPeigipsQEDIRLNGYAIQCRITTEDPANNF-MPDTGRITAYRSAGG-FGIRLDGGnAYTGAVITPYYDSLLVK 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767978886  452 LITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKF 503
Cdd:COG1038   399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
urea_carbox TIGR02712
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ...
63-509 2.57e-179

urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 274264 [Multi-domain]  Cd Length: 1201  Bit Score: 543.09  E-value: 2.57e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886    63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:TIGR02712    1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:TIGR02712   81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:TIGR02712  160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 381
Cdd:TIGR02712  240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   382 LRHKQ--ADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlhlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDR 459
Cdd:TIGR02712  320 PDFASlnISLTPRGAAIEARVYAENPAKNF-QPSPGLLTDVQFP---DDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDR 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767978886   460 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD-VYP 509
Cdd:TIGR02712  396 EDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSfVYT 446
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
61-504 1.55e-177

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 514.30  E-value: 1.55e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  61 KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVH 140
Cdd:PRK12833   3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 141 PGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKA 220
Cdd:PRK12833  83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 221 SAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHgNALWLNERECSIQRRNQKVV 300
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 301 EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKG 379
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 380 YPLRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDR 459
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDF-FPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 767978886 460 TEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
63-504 1.18e-170

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 496.93  E-value: 1.18e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSkSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK07178   2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASA 222
Cdd:PRK07178  81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 223 GGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 302
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 383 RHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEA 462
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDF-LPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 767978886 463 LKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFV 440
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
65-505 6.18e-169

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 491.57  E-value: 6.18e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  65 KILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYG 144
Cdd:PRK08462   6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 145 FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGG 224
Cdd:PRK08462  86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 225 GGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAP 304
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 305 SIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLrH 384
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL-P 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 385 KQADIRINGWAVECRVYAEDPyKSFgLPSIGRLSQYqeplHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTE 461
Cdd:PRK08462 325 SQESIKLKGHAIECRITAEDP-KKF-YPSPGKITKW----IAPGgrnVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 767978886 462 ALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLS 505
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
63-504 6.10e-146

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 433.86  E-value: 6.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTsKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:PRK08463   2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 143 YGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRI-AREIGYPVMIKAS 221
Cdd:PRK08463  81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 222 AGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 301
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 302 EAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYP 381
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 382 LRHKQADIRINGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTE 461
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNF-IPSPGKITEYYPALG-PSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 767978886 462 ALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYI 441
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
176-383 2.78e-102

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: 311.55  E-value: 2.78e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  176 DKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGD 255
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  256 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTV 335
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767978886  336 EFLVDSK-KNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLR 383
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
63-170 1.98e-62

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: 203.10  E-value: 1.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   63 FDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPG 142
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
                          90       100
                  ....*....|....*....|....*...
gi 767978886  143 YGFLSENKEFARCLAAEDVVFIGPDTHA 170
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
123-377 5.53e-58

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: 197.02  E-value: 5.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 123 NMDAIMEAIKKTRAQavHPGYGFLSENkEFARCLAAEdVV----FIGPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgV 198
Cdd:COG0439    1 DIDAIIAAAAELARE--TGIDAVLSES-EFAVETAAE-LAeelgLPGPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 199 VKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDk 278
Cdd:COG0439   75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 279 HGNALWlnereCSIQRRNQK---VVE---EAPSIfLDAETRRAMGEQAVALARAVKYS-SAGTVEFLVDSKKNFYFLEMN 351
Cdd:COG0439  153 DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEIN 226
                        250       260
                 ....*....|....*....|....*...
gi 767978886 352 TRLQVEH--PVTECITGLDLVQEMIRVA 377
Cdd:COG0439  227 ARLGGEHipPLTELATGVDLVREQIRLA 254
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
397-504 1.18e-49

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 168.75  E-value: 1.18e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   397 ECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 476
Cdd:smart00878   1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78
                           90       100
                   ....*....|....*....|....*...
gi 767978886   477 GVTHNIALLREVIINSRFVKGDISTKFL 504
Cdd:smart00878  79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
397-506 3.59e-49

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 167.67  E-value: 3.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  397 ECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 476
Cdd:pfam02785   1 EARIYAEDPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIE 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 767978886  477 GVTHNIALLREVIINSRFVKGDISTKFLSD 506
Cdd:pfam02785  79 GVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
525-633 1.88e-25

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 101.94  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  525 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 604
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
                          90       100
                  ....*....|....*....|....*....
gi 767978886  605 VSVDGTQRTVQClSREAGGnMSIQFLGTV 633
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTS 106
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
75-353 2.99e-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: 88.78  E-value: 2.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  75 ACRVIRtckKMGIKTVAIHS-------DVDassvhvkMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG--- 144
Cdd:COG0458   21 ACKALR---EEGYEVILVNSnpetvstDYD-------TAD-RLYFEP-------LTVEDVLDIIEKEKPDGVIVQFGgqt 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 145 ------FLSENKEFarclaaEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIG 213
Cdd:COG0458   83 alnlavELEEAGIL------EGVKILGTSPDAI----DLAEdrelfKELL-DKLGIPQPKS--GTATSVEEALAIAEEIG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 214 YPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSsqeaassfGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnere 289
Cdd:COG0458  150 YPVIVRPSYVLGGRGMGIVYNEEEleeyLERALKVS--------PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV---- 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767978886 290 CSIQrrNqkvVEEA-----------PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 353
Cdd:COG0458  218 GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
78-383 5.23e-15

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: 79.27  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886    78 VIRTCKKMGIKTVAIHSDVDASSVHVKMADeavcvgpaptsKSY---LNMDAIMEAIKKTRAQAVHPGYGFLSENKeFAR 154
Cdd:TIGR01369  580 AVLALRELGYETIMINYNPETVSTDYDTSD-----------RLYfepLTFEDVMNIIELEKPEGVIVQFGGQTPLN-LAK 647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   155 CLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGM 229
Cdd:TIGR01369  648 ALEEAGVPILGTSPESI----DRAEdrekfSELL-DELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   230 RIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPRHIEIQVLGDkHGNALwlnerECSIQRRnqkvVEEA------ 303
Cdd:TIGR01369  721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVL-----IPGIMEH----IEEAgvhsgd 786
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   304 -----PSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAK 378
Cdd:TIGR01369  787 stcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865

                   ....*
gi 767978886   379 GYPLR 383
Cdd:TIGR01369  866 GKKLE 870
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
126-352 6.00e-14

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: 73.22  E-value: 6.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 126 AIMEAIKKTRAQAVhpgyGFLSENKEFARCLAAE--DVVFI--------------------------GPDTHAIqAMgDK 177
Cdd:COG1181   23 AVAAALDKAGYDVV----PIGIDVEDLPAALKELkpDVVFPalhgrggedgtiqgllellgipytgsGVLASAL-AM-DK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 178 IESKLLAKKAEVNTIPGFdgVVKDAEEAV--RIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgD 255
Cdd:COG1181   97 ALTKRVLAAAGLPTPPYV--VLRRGELADleAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAAL-----EEAFKY-D 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 256 DRLLIEKFIDnPRHIEIQVLGDKHGNALWLNErecsIQRRN-----------QKVVEEAPSIfLDAETRRAMGEQAVALA 324
Cdd:COG1181  169 DKVLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEELEERIQELALKAF 242
                        250       260
                 ....*....|....*....|....*...
gi 767978886 325 RAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:COG1181  243 RALGCRGYARVDFRLDEDGEPYLLEVNT 270
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
78-354 1.26e-12

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 69.96  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  78 VIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVcVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGY----GFLSENKEFA 153
Cdd:COG3919   20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVV-VVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 154 rclaAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKASaggggkgMRIAW 233
Cdd:COG3919   99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPA-------DSVGY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 234 DD---EETRDGFRLSSQEA------ASSFGDDRLLIEKFIDNPRHIEIQVLG--DKHGNALWLnereCSIQRRNQKVVEE 302
Cdd:COG3919  166 DElsfPGKKKVFYVDDREEllallrRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAG 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767978886 303 APSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRL 354
Cdd:COG3919  242 GNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRF 294
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
173-352 2.62e-12

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 68.21  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 173 AMgDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEaass 252
Cdd:PRK01372  96 AM-DKLRTKLVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKY---- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 253 fgDDRLLIEKFIDNPrhiEIQ--VLGDKhgnALwlnerecsiqrrnqKVVE-EAPSIF-------------------LDA 310
Cdd:PRK01372 169 --DDEVLVEKYIKGR---ELTvaVLGGK---AL--------------PVIEiVPAGEFydyeakylaggtqyicpagLPA 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767978886 311 ETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:PRK01372 227 EIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
carB PRK05294
carbamoyl-phosphate synthase large subunit;
153-353 1.98e-09

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 61.27  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  153 ARCLAAEDVVFIGPDTHAIqamgDKIE-----SKLLaKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKAS------ 221
Cdd:PRK05294  646 AKALEAAGVPILGTSPDAI----DLAEdrerfSKLL-EKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSyvlggr 718
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  222 AggggkgMRIAWDDEETRDGFRlssqEAASSFGDDRLLIEKFIDNPRHIEIQVLGDK----------Hgnalwlnerecs 291
Cdd:PRK05294  719 A------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGAIEVDVDAICDGedvliggimeH------------ 776
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767978886  292 iqrrnqkvVEEA-----------PSIFLDAETRRAMGEQAVALARA--VKyssaG--TVEFLVDSKKnFYFLEMNTR 353
Cdd:PRK05294  777 --------IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALElnVV----GlmNVQFAVKDDE-VYVIEVNPR 840
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
164-379 2.79e-09

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 60.75  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  164 IGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEEtrdgfr 243
Cdd:PRK12815  658 LGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA------ 729
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  244 LSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDkhGNALWLN---ERecsiqrrnqkvVEEA-----------PSIFLD 309
Cdd:PRK12815  730 LEAYLAENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiEH-----------IEQAgvhsgdsiavlPPQSLS 795
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  310 AETRRAMGEQAVALARAVKYSSAGTVEFLVDSkKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKG 379
Cdd:PRK12815  796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
58-354 9.86e-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: 58.86  E-value: 9.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886    58 PNEKTFDKILVANRGEI----AC-------RVIRTCKKMGIKTVAIHSDVDASSVHVKMADEaVCVGPaptsksyLNMDA 126
Cdd:TIGR01369    1 PKRTDIKKILVIGSGPIvigqAAefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADK-VYIEP-------LTPEA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   127 IMEAIKKTRAQAVHPGYG-----FLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKD 201
Cdd:TIGR01369   73 VEKIIEKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESE--IAHS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   202 AEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEE----TRDGFRLSSQeaassfgdDRLLIEKFIDNPRHIEIQVLGD 277
Cdd:TIGR01369  151 VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREElkeiAERALSASPI--------NQVLVEKSLAGWKEIEYEVMRD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   278 KHGNALWLnereCSIQrrN----------QKVVeeAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSK-KNFY 346
Cdd:TIGR01369  223 SNDNCITV----CNME--NfdpmgvhtgdSIVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYY 294

                   ....*...
gi 767978886   347 FLEMNTRL 354
Cdd:TIGR01369  295 VIEVNPRV 302
ddl PRK01966
D-alanine--D-alanine ligase;
163-352 5.57e-07

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 52.05  E-value: 5.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 163 FIGPDTHAiQAMG-DKIESKLLAKKAEVNTIPGfdgVV---KDAEEAV--RIAREIGYPVMIKASaggggkgmriawdde 236
Cdd:PRK01966 110 YVGCGVLA-SALSmDKILTKRLLAAAGIPVAPY---VVltrGDWEEASlaEIEAKLGLPVFVKPA--------------- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 237 etRDGfrlssqeaaSSFG--------------------DDRLLIEKFIdNPRHIEIQVLGdkhgnalwlNERECSiqrrn 296
Cdd:PRK01966 171 --NLG---------SSVGiskvkneeelaaaldlafeyDRKVLVEQGI-KGREIECAVLG---------NDPKAS----- 224
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767978886 297 qkVVEE--APSIFLD-------------------AETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:PRK01966 225 --VPGEivKPDDFYDyeakyldgsaeliipadlsEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
PLN02735 PLN02735
carbamoyl-phosphate synthase
166-281 1.52e-06

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 51.70  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  166 PDThaIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRdgfrlS 245
Cdd:PLN02735  694 PDS--IDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK-----T 764
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767978886  246 SQEAASSFGDDR-LLIEKFIDNPRHIEIQVLGDKHGN 281
Cdd:PLN02735  765 YLETAVEVDPERpVLVDKYLSDATEIDVDALADSEGN 801
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
156-382 1.91e-06

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 51.51  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  156 LAAEDVVFIGPDTHAIQAMGDKIESKLLAKKaevNTIP-GFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWD 234
Cdd:PRK12815  108 LEQYGVELLGTNIEAIQKGEDRERFRALMKE---LGEPvPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAEN 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  235 DEETRDGFRlsSQEAASSFGDdrLLIEKFIDNPRHIEIQVLGDKHGNALWLNERE----CSIQRRNQKVVeeAPSIFL-D 309
Cdd:PRK12815  185 LEELEQLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVCNMEnidpVGIHTGDSIVV--APSQTLtD 258
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767978886  310 AETRRaMGEQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPL 382
Cdd:PRK12815  259 DEYQM-LRSASLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTL 331
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
105-353 2.90e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 49.88  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 105 MADEAVcVGPAPTSKSYLnmDAIMEAIKKTRAQAVHPGY----GFLSENKEfarCLAAEDVVFIGPDTHAIQAMGDKIES 180
Cdd:PRK12767  42 FADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLT 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 181 KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG------FRLSSQEAASSFG 254
Cdd:PRK12767 116 YEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKP------------------RDGsasigvFKVNDKEELEFLL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 255 DDR--LLIEKFIDNPRhIEIQVLGDKHGNALwlnereCSIQRR---------NQKVVEEAPSIFldaetrramgEQAVAL 323
Cdd:PRK12767 178 EYVpnLIIQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKrievragetSKGVTVKDPELF----------KLAERL 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 767978886 324 ARAVKYSSAGTVEFLVDSKKnFYFLEMNTR 353
Cdd:PRK12767 241 AEALGARGPLNIQCFVTDGE-PYLFEINPR 269
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
211-352 3.18e-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: 48.47  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  211 EIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrlssqEAASSFgDDRLLIEKFIDNpRHIEIQVLGDKHGNALWLNER-- 288
Cdd:pfam07478  34 ALGYPVFVKPARLGSSVGVSKVESREELQAAI-----EEAFQY-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvp 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767978886  289 ECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALA----RAVKYSSAGTVEFLVDSKKNFYFLEMNT 352
Cdd:pfam07478 107 SGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELAlkayKALGCRGLARVDFFLTEDGEIVLNEVNT 174
carB PRK05294
carbamoyl-phosphate synthase large subunit;
75-282 1.61e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 48.55  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886   75 ACRVIRtckKMGIKTVAIHSDV-----DAssvhvKMADeAVCVGPaptsksyLNMDAIMEAIKKTRAQAVHPGYG----- 144
Cdd:PRK05294   33 ACKALR---EEGYRVVLVNSNPatimtDP-----EMAD-ATYIEP-------ITPEFVEKIIEKERPDAILPTMGgqtal 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  145 ----FLSENKEFARClaaeDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIka 220
Cdd:PRK05294   97 nlavELAESGVLEKY----GVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVII-- 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767978886  221 saggggkgmR-----------IAWDDEETRD----GFRLS--SQeaassfgddrLLIEKFIDNPRHIEIQVLGDKHGNA 282
Cdd:PRK05294  169 ---------RpsftlggtgggIAYNEEELEEiverGLDLSpvTE----------VLIEESLLGWKEYEYEVMRDKNDNC 228
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
83-350 3.37e-05

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: 46.61  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  83 KKMGIKTVAIHSDVDASSVHVkmADEAVcVGPaptsksYLNMDAIMEAIKktRAQAVhpgyGFLSEN--KEFARCLAAED 160
Cdd:COG0026   11 KRLGYRVHVLDPDPDSPAAQV--ADEHI-VAD------YDDEEALREFAE--RCDVV----TFEFENvpAEALEALEAEV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 161 VVFigPDTHAIQAMGDKIESKLLAKKAEVNTiPGFDgVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeeTRD 240
Cdd:COG0026   76 PVR--PGPEALEIAQDRLLEKAFLAELGIPV-APFA-AVDSLEDLEAAIAELGLPAVLKT-----------------RRG 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 241 G------FRLSSQE----AASSFGDDRLLIEKFIDNPRhiEIQVLG--DKHGN-ALW---LNerecsIQRRNQKVVEEAP 304
Cdd:COG0026  135 GydgkgqVVIKSAAdleaAWAALGGGPCILEEFVPFER--ELSVIVarSPDGEvATYpvvEN-----VHRNGILDESIAP 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 767978886 305 SiFLDAETRRAMGEQAVALARAVKYssAGT--VEFLVDSKKNFYFLEM 350
Cdd:COG0026  208 A-RISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGELLVNEI 252
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
152-375 7.62e-05

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: 45.32  E-value: 7.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 152 FARCLAAEDVVFIgPDTHAIQAMGDKIESKLLAKKAEVNTIPGFdgVVKDAEEAVRIAREIGYPVMIKasaggggkgmri 231
Cdd:COG0189   73 LLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVLK------------ 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 232 awddeeTRDG------FRLSSQEAASSF-------GDDRLLIEKFIDNPRHIEIQ--VLGDK----------HGnalwln 286
Cdd:COG0189  138 ------PLDGsggrgvFLVEDEDALESIlealtelGSEPVLVQEFIPEEDGRDIRvlVVGGEpvaairripaEG------ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 287 erECSIQRRNQKVVEEAPsifLDAETRramgEQAVALARAVKYSSAGtVEFLVDsKKNFYFLEMNtrlqvehpVTECI-- 364
Cdd:COG0189  206 --EFRTNLARGGRAEPVE---LTDEER----ELALRAAPALGLDFAG-VDLIED-DDGPLVLEVN--------VTPGFrg 266
                        250
                 ....*....|....*
gi 767978886 365 ----TGLDLVQEMIR 375
Cdd:COG0189  267 leraTGVDIAEAIAD 281
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
83-265 2.24e-04

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 43.99  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  83 KKMGIKTVAIhsDVDASSVHVKMADEAVCVgpaptskSYLNMDAIMEAIKktRAQAVhpGYGFlsEN--KEFARCLAAED 160
Cdd:PRK06019  22 APLGYKVIVL--DPDPDSPAAQVADEVIVA-------DYDDVAALRELAE--QCDVI--TYEF--ENvpAEALDALAARV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 161 VVFIGPDthAIQAMGDKIESKLLAKKAEVNTiPGFdGVVKDAEEAVRIAREIGYPVMIKasaggggkgmriawddeeTR- 239
Cdd:PRK06019  87 PVPPGPD--ALAIAQDRLTEKQFLDKLGIPV-APF-AVVDSAEDLEAALADLGLPAVLK------------------TRr 144
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767978886 240 ---DG---FRLSS----QEAASSFGDDRLLIEKFID 265
Cdd:PRK06019 145 ggyDGkgqWVIRSaedlEAAWALLGSVPCILEEFVP 180
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
179-220 3.84e-04

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 43.57  E-value: 3.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767978886 179 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIKA 220
Cdd:COG1042  492 EAKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
PLN02735 PLN02735
carbamoyl-phosphate synthase
129-389 3.99e-04

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 44.00  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  129 EAIKKTRAQAVHPGYG---FLSENKEFAR--CLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPgfDGVVKDAE 203
Cdd:PLN02735   92 QVIAKERPDALLPTMGgqtALNLAVALAEsgILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLD 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  204 EAVRIAREIG-YPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSfgddRLLIEKFIDNPRHIEIQVLGDKHGNA 282
Cdd:PLN02735  170 ECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELEVMRDLADNV 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886  283 LWLnereCSIQRRNQKVVEEAPSI-------FLDAETRRaMGEQAVALARAVKYSSAGT-VEFLVDSKK-NFYFLEMNTR 353
Cdd:PLN02735  246 VII----CSIENIDPMGVHTGDSItvapaqtLTDKEYQR-LRDYSVAIIREIGVECGGSnVQFAVNPVDgEVMIIEMNPR 320
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767978886  354 LQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADI 389
Cdd:PLN02735  321 VSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDI 356
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
179-219 7.33e-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: 41.69  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767978886  179 ESKLLAKKAEVNTIPGfdGVVKDAEEAVRIAREIGYPVMIK 219
Cdd:pfam13549  14 EAKALLAAYGIPVVPT--RLARSPEEAVAAAEEIGYPVVLK 52
PRK14016 PRK14016
cyanophycin synthetase; Provisional
197-264 1.78e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 41.68  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978886 197 GVVKDAEEAVRIAREIGYPVMIKAsaggggkgmriawddeetRDG-------FRLSSQE-------AASSFGDDrLLIEK 262
Cdd:PRK14016 233 RVVTSAEDAWEAAEEIGYPVVVKP------------------LDGnhgrgvtVNITTREeieaayaVASKESSD-VIVER 293

                 ..
gi 767978886 263 FI 264
Cdd:PRK14016 294 YI 295
 
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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