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Conserved domains on  [gi|2030402101|dbj|GIQ93388|]
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acetyl-CoA carboxylase, biotin carboxylase subunit [Lactiplantibacillus plantarum]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-458 0e+00

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


:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 719.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:COG4770     1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIkaa 160
Cdd:COG4770    81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIkas 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 aggggkgIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:COG4770   161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:COG4770   241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPMGtLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:COG4770   321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDFLKGWLSDAQAQV 458
Cdd:COG4770   400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-458 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 719.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:COG4770     1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIkaa 160
Cdd:COG4770    81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIkas 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 aggggkgIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:COG4770   161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:COG4770   241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPMGtLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:COG4770   321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDFLKGWLSDAQAQV 458
Cdd:COG4770   400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-447 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 673.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK08591    1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:PRK08591   81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:PRK08591  161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:PRK08591  241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLiYPMGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:PRK08591  321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRY-HPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDFL 447
Cdd:PRK08591  400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLA 446
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-444 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: 554.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPmGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPP-GGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-321 9.40e-67

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: 212.94  E-value: 9.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 115 DKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDD 194
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 195 HRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLEESPCAVITTAERTELGQLVADATKKLGYTNTGTY 274
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2030402101 275 EFLMDQ-QHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMPL 321
Cdd:pfam02786 161 EFALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-443 1.94e-46

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: 156.03  E-value: 1.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  336 ECRLNAEDPYHDFRPQPGKITRLIYPMGtLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMVSRKMHRCLLELTIDG 415
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79

                           90       100
                   ....*....|....*....|....*...
gi 2030402101  416 VQTNRIFLAGLVADSTVGRGTYTTAYIE 443
Cdd:smart00878  80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-458 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 719.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:COG4770     1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIkaa 160
Cdd:COG4770    81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIkas 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 aggggkgIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:COG4770   161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:COG4770   241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPMGtLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:COG4770   321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDFLKGWLSDAQAQV 458
Cdd:COG4770   400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-447 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 673.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK08591    1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:PRK08591   81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:PRK08591  161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:PRK08591  241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLiYPMGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:PRK08591  321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRY-HPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDFL 447
Cdd:PRK08591  400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLA 446
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-448 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 588.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK05586    1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:PRK05586   81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:PRK05586  161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:PRK05586  241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPmGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:PRK05586  321 LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIP-GGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDFLK 448
Cdd:PRK05586  400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLVD 447
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 562.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK08654    1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:PRK08654   81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:PRK08654  161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQhHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:PRK08654  241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNG-NFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPmGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:PRK08654  320 LSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:PRK08654  399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 560.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK06111    1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:PRK06111   81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:PRK06111  161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:PRK06111  241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPyHDFRPQPGKITRLIYPMGTlGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:PRK06111  321 LSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGE-GVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:PRK06111  399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-444 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: 554.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPmGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPP-GGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-444 8.09e-178

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 528.17  E-value: 8.09e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101    1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGA--SPVnQSYLNMQAIISAANLTGCQAI 78
Cdd:PRK12999     4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEgkHPV-RAYLDIDEIIRVAKQAGVDAI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   79 HPGYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIK 158
Cdd:PRK12999    83 HPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  159 AAAGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKV 238
Cdd:PRK12999   163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  239 LEESPCAVITTAERTElgqLVADA---TKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQI 315
Cdd:PRK12999   243 VEIAPAPGLSEELRER---ICEAAvklARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  316 AAGMPL------KIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPMGtLGVRIDAGVV-TGSMIAPFYDSMIA 388
Cdd:PRK12999   320 AEGATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLLV 398

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2030402101  389 KIIVHGINRKMVSRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:PRK12999   399 KLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-444 3.92e-177

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: 526.57  E-value: 3.92e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101    1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGA--SPVnQSYLNMQAIISAANLTGCQAI 78
Cdd:COG1038      3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEgkGPV-DAYLDIEEIIRVAKEKGVDAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   79 HPGYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIK 158
Cdd:COG1038     82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  159 AAAGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKV 238
Cdd:COG1038    162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  239 LEESPCAVITTAERTElgqLVADA---TKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQI 315
Cdd:COG1038    242 VEIAPAPNLDEELREA---ICEAAvklAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  316 AAGMPL-----KIK-QADVKIHGVAMECRLNAEDPYHDFRPQPGKITrlIY--PMGtLGVRIDAGVV-TGSMIAPFYDSM 386
Cdd:COG1038    319 AEGYSLddpeiGIPsQEDIRLNGYAIQCRITTEDPANNFMPDTGRIT--AYrsAGG-FGIRLDGGNAyTGAVITPYYDSL 395

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2030402101  387 IAKIIVHGINRKMVSRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:COG1038    396 LVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDE 453
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 3-458 3.21e-176

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 501.98  E-value: 3.21e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   3 KKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHPGY 82
Cdd:PRK12833    6 RKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  83 GFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAAAG 162
Cdd:PRK12833   86 GFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 163 GGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQgHVIYLPERDCSLQRNHQKVLEES 242
Cdd:PRK12833  166 GGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 243 PCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQH-HFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMPL 321
Cdd:PRK12833  245 PSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARgEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 322 KIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPMGTlGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMVS 401
Cdd:PRK12833  325 RFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGP-GVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2030402101 402 RKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQdflkgWLSDAQAQV 458
Cdd:PRK12833  404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEA-----WLAEWRAAL 455
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-443 5.80e-174

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 496.55  E-value: 5.80e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVnQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK07178    1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAA 160
Cdd:PRK07178   80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 161 AGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLE 240
Cdd:PRK07178  160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 241 ESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMP 320
Cdd:PRK07178  240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 321 LKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLIYPMGTlGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMV 400
Cdd:PRK07178  320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGP-GVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2030402101 401 SRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIE 443
Cdd:PRK07178  399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
3-446 2.27e-167

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 478.47  E-value: 2.27e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   3 KKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHPGY 82
Cdd:PRK08462    5 KRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  83 GFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAAAG 162
Cdd:PRK08462   85 GFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 163 GGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLEES 242
Cdd:PRK08462  165 GGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEES 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 243 PCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMPLk 322
Cdd:PRK08462  245 PAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL- 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 323 IKQADVKIHGVAMECRLNAEDPyHDFRPQPGKITRLIYPMGTlGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMVSR 402
Cdd:PRK08462  324 PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGR-NVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2030402101 403 KMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQDF 446
Cdd:PRK08462  402 KMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEHF 445
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-444 3.53e-156

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 451.57  E-value: 3.53e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   1 MFKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVnQSYLNMQAIISAANLTGCQAIHP 80
Cdd:PRK08463    1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  81 GYGFLSENAEFAKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSPSVLKD-VEAAMQAAHTLGYPVMIKA 159
Cdd:PRK08463   80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSEsMEEIKIFARKIGYPVILKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 160 AAGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVL 239
Cdd:PRK08463  160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 240 EESPCAVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGM 319
Cdd:PRK08463  240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 320 PLKIKQADVKIHGVAMECRLNAEDPYHDFRPQPGKITRLiYPMGTLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKM 399
Cdd:PRK08463  320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEY-YPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2030402101 400 VSRKMHRCLLELTIDGVQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:PRK08463  399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-321 9.40e-67

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: 212.94  E-value: 9.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 115 DKENARQTMQRLGVPVIPGSPSVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDD 194
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 195 HRLYLEKIIAPAKHIEVQVLADQQGHVIYLPERDCSLQRNHQKVLEESPCAVITTAERTELGQLVADATKKLGYTNTGTY 274
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2030402101 275 EFLMDQ-QHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGMPL 321
Cdd:pfam02786 161 EFALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-109 2.00e-60

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: 192.70  E-value: 2.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   2 FKKVLVANRGEIAVQVIRALHEMGIKAVAVYSVADQESLFVHLADEAVCIGASPVNQSYLNMQAIISAANLTGCQAIHPG 81
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 2030402101  82 YGFLSENAEFAKMCADCQLTFIGPRPEV 109
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 62-320 5.33e-51

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: 173.52  E-value: 5.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  62 NMQAIISAAnltgcQAIHPGYGF---LSENAE----FAKMCADCQLTfiGPRPEVIDQMGDKENARQTMQRLGVPViPGS 134
Cdd:COG0439     1 DIDAIIAAA-----AELARETGIdavLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 135 pSVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRTAQQEAQASYDDHRLYLEKIIaPAKHIEVQVL 214
Cdd:COG0439    73 -ALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFL-EGREYSVEGL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 215 AdQQGHVIYlperdCSLQRNHQK---VLE---ESPcAVITTAERTELGQLVADATKKLGYTN-TGTYEFLMDQQHHFYFL 287
Cdd:COG0439   151 V-RDGEVVV-----CSITRKHQKppyFVElghEAP-SPLPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLI 223

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2030402101 288 EMNTRLQVEH--TVTEMVTGIELIKAQVQIAAGMP 320
Cdd:COG0439   224 EINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-443 1.94e-46

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: 156.03  E-value: 1.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  336 ECRLNAEDPYHDFRPQPGKITRLIYPMGtLGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMVSRKMHRCLLELTIDG 415
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79

                           90       100
                   ....*....|....*....|....*...
gi 2030402101  416 VQTNRIFLAGLVADSTVGRGTYTTAYIE 443
Cdd:smart00878  80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-444 1.48e-43

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: 148.80  E-value: 1.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 336 ECRLNAEDPYHDFRPQPGKITRLIYPMGTlGVRIDAGVVTGSMIAPFYDSMIAKIIVHGINRKMVSRKMHRCLLELTIDG 415
Cdd:pfam02785   1 EARIYAEDPDNNFLPSPGKVTRYRFPGGP-GVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79

                          90       100
                  ....*....|....*....|....*....
gi 2030402101 416 VQTNRIFLAGLVADSTVGRGTYTTAYIEQ 444
Cdd:pfam02785  80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 92-322 2.18e-10

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: 63.09  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   92 AKMCADCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGspSVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAV 171
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  172 SNDQDLAKAFRtaqqEAQASYDDHRLYLEKIIAPAKHIEVQVLADqqGHVIYLP------ER------DCSLQRNHQKVL 239
Cdd:TIGR01369  724 YNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEEVLIPgimehiEEagvhsgDSTCVLPPQTLS 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  240 EEspcavitTAERTElgQLVADATKKLGYTNTGTYEFLMDqQHHFYFLEMNTRLQVEHTVTEMVTGIELIKAQVQIAAGM 319
Cdd:TIGR01369  798 AE-------IVDRIK--DIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGK 867


                   ...
gi 2030402101  320 PLK 322
Cdd:TIGR01369  868 KLE 870
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 103-222 3.51e-10

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: 61.82  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 103 IGPRPEVIDQMGDKENARQTMQRLGVPVIPGSpsVLKDVEAAMQAAHTLGYPVMikaaaggggkgIRA-----------V 171
Cdd:COG0458   102 LGTSPDAIDLAEDRELFKELLDKLGIPQPKSG--TATSVEEALAIAEEIGYPVI-----------VRPsyvlggrgmgiV 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2030402101 172 SNDQDLAKAFRTAqqeAQASyDDHRLYLEKIIAPAKHIEVQVLADQQGHVI 222
Cdd:COG0458   169 YNEEELEEYLERA---LKVS-PDHPVLIDESLLGAKEIEVDVVRDGEDNVI 215
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
4-293 1.87e-08

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 56.09  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   4 KVLVANRGEIAVQVIRALHEMGIKAVAV---------YS------------VADQESLFVHLADEAVCIGAS---PVNQS 59
Cdd:COG3919     7 RVVVLGGDINALAVARSLGEAGVRVIVVdrdplgpaaRSryvdevvvvpdpGDDPEAFVDALLELAERHGPDvliPTGDE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  60 YLNmqaiisaanltgcqaihpgygFLSEN-AEFAKmcadcQLTFIGPRPEVIDQMGDKENARQTMQRLGVPViPGSpSVL 138
Cdd:COG3919    87 YVE---------------------LLSRHrDELEE-----HYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKT-VVL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 139 KDVEAAMQAAHTLGYPVMI--------KAAAGGGGKGIRAVSNDQDLAKAFRTAQQEaqasydDHRLYL-EKIIAPAKHI 209
Cdd:COG3919   139 DSADDLDALAEDLGFPVVVkpadsvgyDELSFPGKKKVFYVDDREELLALLRRIAAA------GYELIVqEYIPGDDGEM 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 210 E-VQVLADQQGHVIYLperdCSlqrnHQKVLEESPC----AVITTAERTELGQLVADATKKLGYTNTGTYEFLMDQQHH- 283
Cdd:COG3919   213 RgLTAYVDRDGEVVAT----FT----GRKLRHYPPAggnsAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGe 284

                         330
                  ....*....|
gi 2030402101 284 FYFLEMNTRL 293
Cdd:COG3919   285 YKLIEINPRF 294
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 97-322 2.24e-07

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 53.43  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101   97 DCQLTFIGPRPEVIDQMGDKENARQTMQRLGVPVIPGSpsVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQD 176
Cdd:PRK12815   652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL--TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  177 LAKAFRTAqqeaqASYDDHRL---YLEkiiapAKHIEVQVLADqqGHVIYLP------ER------DC-------SLQRN 234
Cdd:PRK12815   730 LEAYLAEN-----ASQLYPILidqFID-----GKEYEVDAISD--GEDVTIPgiiehiEQagvhsgDSiavlppqSLSEE 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  235 HQKVLEESPCAVIttaertelgqlvadatKKLGYTNTGTYEFLMdQQHHFYFLEMNTRlqVEHTV--TEMVTGIELIKAQ 312
Cdd:PRK12815   798 QQEKIRDYAIKIA----------------KKLGFRGIMNIQFVL-ANDEIYVLEVNPR--ASRTVpfVSKATGVPLAKLA 858

                          250
                   ....*....|
gi 2030402101  313 VQIAAGMPLK 322
Cdd:PRK12815   859 TKVLLGKSLA 868
carB PRK05294
carbamoyl-phosphate synthase large subunit;
102-157 1.09e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 48.17  E-value: 1.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2030402101  102 FIGPRPEVIDQMGDKENARQTMQRLGVPVIPGspSVLKDVEAAMQAAHTLGYPVMI 157
Cdd:PRK05294   115 LIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVII 168
PLN02735 PLN02735
carbamoyl-phosphate synthase
 104-222 1.26e-05

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 47.85  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  104 GPRPEVIDQMGDKENARQTMQRLGVPVIPGSpsVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRT 183
Cdd:PLN02735   691 GTSPDSIDAAEDRERFNAILNELKIEQPKGG--IARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLET 768

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2030402101  184 AQQeaqasYDDHRLYL-EKIIAPAKHIEVQVLADQQGHVI 222
Cdd:PLN02735   769 AVE-----VDPERPVLvDKYLSDATEIDVDALADSEGNVV 803
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 103-222 2.35e-05

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: 46.92  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  103 IGPRPEVIDQMGDKENARQTMQRLGVPVIPGSpsVLKDVEAAMQAAHTLGYPVMikaaaggggkgIRA-----------V 171
Cdd:TIGR01369  115 LGTPVEAIKKAEDRELFREAMKEIGEPVPESE--IAHSVEEALAAAKEIGYPVI-----------VRPaftlggtgggiA 181

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2030402101  172 SNDQDL----AKAFRtaqqeaqASYDDHRLyLEKIIAPAKHIEVQVLADQQGHVI 222
Cdd:TIGR01369  182 YNREELkeiaERALS-------ASPINQVL-VEKSLAGWKEIEYEVMRDSNDNCI 228
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 123-291 7.15e-05

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: 43.84  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 123 MQRLGVPVIP-------GSPSVLKDVEAAMQAAhtLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRTAQQEaqasydDH 195
Cdd:pfam07478   2 LKAAGLPVVPfvtftraDWKLNPKEWCAQVEEA--LGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------DE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 196 RLYLEKIIApAKHIEVQVLADQQGHVIYLPER--DCSLQRNHQKVLEES-----PcAVITTAERTELGQLVADATKKLGY 268
Cdd:pfam07478  74 KVLVEEGIE-GREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvP-ADLEEEQEEQIQELALKAYKALGC 151

                         170       180
                  ....*....|....*....|...
gi 2030402101 269 TNTGTYEFLMDQQHHFYFLEMNT 291
Cdd:pfam07478 152 RGLARVDFFLTEDGEIVLNEVNT 174
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 108-222 3.21e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 39.95  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101  108 EVIdQMG-DKENARQTMQRLGVPViPGSPSVLKdVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRtaqQ 186
Cdd:PRK12815   121 EAI-QKGeDRERFRALMKELGEPV-PESEIVTS-VEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFK---Q 194

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2030402101  187 EAQASyDDHRLYLEKIIAPAKHIEVQVLADQQGHVI 222
Cdd:PRK12815   195 GLQAS-PIHQCLLEESIAGWKEIEYEVMRDRNGNCI 229
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 115-291 6.07e-03

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 38.55  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 115 DKENARQTMQRLGVPVIPGSpsVLKDVEAAMQAAHTLGYPVMIKAAAGGGGKGIRAVSNDQDLAKAFRTAqqeaqASYDD 194
Cdd:PRK01372   98 DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELA-----FKYDD 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030402101 195 HRLyLEKIIaPAKHIEVQVLADQQGHVI--------------YLPErdcslqrnhqKVLEESPCAvITTAERTELGQLVA 260
Cdd:PRK01372  171 EVL-VEKYI-KGRELTVAVLGGKALPVIeivpagefydyeakYLAG----------GTQYICPAG-LPAEIEAELQELAL 237

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2030402101 261 DATKKLGYTNTGTYEFLMDQQHHFYFLEMNT 291
Cdd:PRK01372  238 KAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
 
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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