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Conserved domains on  [gi|488138861|ref|WP_002210069|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxylase subunit [Yersinia pseudotuberculosis complex]

Protein Classification

acetyl-CoA carboxylase biotin carboxylase subunit( domain architecture ID 11483369)

acetyl-CoA carboxylase biotin carboxylase subunit catalyzes the carboxylation of the carrier protein

EC:  6.-.-.-
Gene Ontology:  GO:0005524|GO:0016874
PubMed:  18725455|21592965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


:

Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 910.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLsDDTTKNKAFAKRIGYPVIIKA 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLGLQET 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 910.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLsDDTTKNKAFAKRIGYPVIIKA 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLGLQET 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-448 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: 793.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGpLSDDTTKNKAFAKRIGYPVIIKA 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 488138861  399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLGLQE 448
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMGE 449
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-444 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 779.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTTKnKAFAKRIGYPVIIKA 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEA-LAIAEEIGYPVLIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SgggggrgmrvvRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:COG4770  160 SaggggkgmrvvRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:COG4770  240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:COG4770  320 PLPFTQEDIKLRGHAIECRINAEDPaRGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKL 444
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-322 7.01e-94

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: 281.89  E-value: 7.01e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  115 DKVSAISAMKKAGVPCVPGSDGPLSDDTtKNKAFAKRIGYPVIIKASGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFN 194
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEE-EALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  195 NDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITSEMRRYIGERCAKACMEIGYRGAGT 274
Cdd:pfam02786  80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488138861  275 FEFLYE--NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQPLS 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-441 8.96e-60

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: 190.70  E-value: 8.96e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVAIARMKNALAELIIDGI 414
Cdd:smart00878   1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 488138861   415 KTNVELQQRIMNDENFQHGGTNIHYLE 441
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 910.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLsDDTTKNKAFAKRIGYPVIIKA 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLGLQET 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-448 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: 793.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGpLSDDTTKNKAFAKRIGYPVIIKA 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 488138861  399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLGLQE 448
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMGE 449
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-444 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 779.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTTKnKAFAKRIGYPVIIKA 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEA-LAIAEEIGYPVLIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SgggggrgmrvvRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:COG4770  160 SaggggkgmrvvRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:COG4770  240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:COG4770  320 PLPFTQEDIKLRGHAIECRINAEDPaRGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKL 444
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
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: 679.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK06111   1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTtKNKAFAKRIGYPVIIKA 160
Cdd:PRK06111  81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAE-EAIAIARQIGYPVMLKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYENGE-FYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVAI 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 488138861 400 ARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKL 444
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQL 444
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 659.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK08654   1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTTKnKAFAKRIGYPVIIKA 160
Cdd:PRK08654  81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEA-KEIAEEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQP 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 321 LSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVAI 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 488138861 400 ARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLGLQET 449
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEE 449
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 607.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK05586   1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTTKNKaFAKRIGYPVIIKA 160
Cdd:PRK05586  81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALE-IAKEIGYPVMVKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPkNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLG 445
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-433 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 582.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAVH 79
Cdd:PRK12999    4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   80 PGYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPlSDDTTKNKAFAKRIGYPVIIK 159
Cdd:PRK12999   84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP-IDDIEEALEFAEEIGYPIMLK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  160 ASGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK12999  163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  240 VEEAPAPGITSEMRRYIgerCAKA---CMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRI 315
Cdd:PRK12999  243 VEIAPAPGLSEELRERI---CEAAvklARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  316 AAGQPLS------IKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGK 387
Cdd:PRK12999  320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPaNNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVK 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 488138861  388 LITYGENRDVAIARMKNALAELIIDGIKTNVELQQRIMNDENFQHG 433
Cdd:PRK12999  400 LTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG 445
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-433 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: 570.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAVH 79
Cdd:COG1038     3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGpVDAYLDIEEIIRVAKEKGVDAIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   80 PGYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTTKnKAFAKRIGYPVIIK 159
Cdd:COG1038    83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEA-LAFAEEIGYPVMLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  160 ASGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:COG1038   162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  240 VEEAPAPGITSEMRRYIgerCAKA---CMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRI 315
Cdd:COG1038   242 VEIAPAPNLDEELREAI---CEAAvklAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  316 AAGQPLS------IKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRW-ESHIYAGYTVPPYYDSMIGK 387
Cdd:COG1038   319 AEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPaNNFMPDTGRITAYRSAGGFGIRLdGGNAYTGAVITPYYDSLLVK 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 488138861  388 LITYGENRDVAIARMKNALAELIIDGIKTNVELQQRIMNDENFQHG 433
Cdd:COG1038   399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAG 444
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 2-441 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 552.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   2 LDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHPG 81
Cdd:PRK12833   5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  82 YGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDDTTKNKAfAKRIGYPVIIKAS 161
Cdd:PRK12833  85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEV-AARIGYPLMIKAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 162 GGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQgNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 242 EAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLY--ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPlRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLE 441
Cdd:PRK12833 403 LARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
2-443 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 552.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   2 LDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHPG 81
Cdd:PRK08462   4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  82 YGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSdDTTKNKAFAKRIGYPVIIKAS 161
Cdd:PRK08462  84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALK-SYEEAKKIAKEIGYPVILKAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 162 GGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 242 EAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQP 320
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 321 LSiKQDEVKVHGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVAIA 400
Cdd:PRK08462 323 LP-SQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488138861 401 RMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKK 443
Cdd:PRK08462 402 KMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-441 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 545.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK07178   1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLSDdTTKNKAFAKRIGYPVIIKA 160
Cdd:PRK07178  80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLAD-LDEALAEAERIGYPVMLKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYE-NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 320 PLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPkNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 488138861 399 IARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLE 441
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-445 5.25e-175

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 498.57  E-value: 5.25e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAVHP 80
Cdd:PRK08463   1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP-IKGYLDVKRIVEIAKACGADAIHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDgPLSDDTTKN-KAFAKRIGYPVIIK 159
Cdd:PRK08463  80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNSESMEEiKIFARKIGYPVILK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 160 ASGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 240 VEEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAG 318
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 319 QPLSIKQDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDV 397
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVwKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 488138861 398 AIARMKNALAELIIDGIKTNVELQQRIMNDENFQHGGTNIHYLEKKLG 445
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 4-433 2.18e-159

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 480.09  E-value: 2.18e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861     4 KIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPS---VKSYLNIPAIISAAEITGAVAVHP 80
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDlgpIEAYLSIDEIIRVAKLNGVDAIHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    81 GYGFLSENADFAEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGPLsDDTTKNKAFAKRIGYPVIIKA 160
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPP-ETMEEVLDFAAAIGYPVIIKA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   161 SGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR01235  160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   241 EEAPAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLY-ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQ 319
Cdd:TIGR01235  240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   320 PLSIK------QDEVKVHGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGKLITY 391
Cdd:TIGR01235  320 SLPTPqlgvpnQEDIRTNGYAIQCRVTTEDPaNNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 488138861   392 GENRDVAIARMKNALAELIIDGIKTNVELQQRIMNDENFQHG 433
Cdd:TIGR01235  400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-322 7.01e-94

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: 281.89  E-value: 7.01e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  115 DKVSAISAMKKAGVPCVPGSDGPLSDDTtKNKAFAKRIGYPVIIKASGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFN 194
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEE-EALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  195 NDMVYMEKYLENPRHIEVQILADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITSEMRRYIGERCAKACMEIGYRGAGT 274
Cdd:pfam02786  80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488138861  275 FEFLYE--NGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQPLS 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 62-320 1.27e-68

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: 218.97  E-value: 1.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  62 NIPAIISAAEitgavAVHPGYGF---LSENAD----FAEQVERSGFIfiGPRAETIRLMGDKVSAISAMKKAGVPcVPGS 134
Cdd:COG0439    1 DIDAIIAAAA-----ELARETGIdavLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 135 DgpLSDDTTKNKAFAKRIGYPVIIKASGGGGGRGMRVVRHDKDLEESINMTRAEAKAAFNNDMVYMEKYLENpRHIEVQI 214
Cdd:COG0439   73 A--LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 215 LADgQGNAIYlaerdCSMQRRHQK---VVE---EAPAPgITSEMRRYIGERCAKACMEIGY-RGAGTFEFLY-ENGEFYF 286
Cdd:COG0439  150 LVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYL 222

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 488138861 287 IEMNTRIQVEH--TVTEMITGIDLIKEQLRIAAGQP 320
Cdd:COG0439  223 IEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-109 1.97e-61

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: 195.01  E-value: 1.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    2 LDKIVIANRGEIALRILRACKELGIKTVAVHSVADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAVHPG 81
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 488138861   82 YGFLSENADFAEQVERSGFIFIGPRAET 109
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-441 8.96e-60

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: 190.70  E-value: 8.96e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVAIARMKNALAELIIDGI 414
Cdd:smart00878   1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 488138861   415 KTNVELQQRIMNDENFQHGGTNIHYLE 441
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-442 5.45e-57

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: 183.46  E-value: 5.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLITYGENRDVAIARMKNALAELIIDGI 414
Cdd:pfam02785   1 EARIYAEDPdNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80

                          90       100
                  ....*....|....*....|....*...
gi 488138861  415 KTNVELQQRIMNDENFQHGGTNIHYLEK 442
Cdd:pfam02785  81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 92-321 1.21e-12

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


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 70.03  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861    92 AEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGSDGplsddTTKNKA--FAKRIGYPVIIKASGGGGGRGM 169
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTA-----TSVEEAveFASEIGYPVLVRPSYVLGGRAM 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   170 RVVRHDKDLEESINmtraEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIY-LAErdcsmqrrHqkvVEEA----- 243
Cdd:TIGR01369  721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPgIME--------H---IEEAgvhsg 785

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   244 ------PAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAA 317
Cdd:TIGR01369  786 dstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865


                   ....
gi 488138861   318 GQPL 321
Cdd:TIGR01369  866 GKKL 869
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
84-293 6.08e-10

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 60.71  E-value: 6.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  84 FLSENADFAEQversGFIFIGPRAETIRLMGDKVSAISAMKKAGVPC----VPGSDGPLSddttknkAFAKRIGYPVIIK 159
Cdd:COG3919   90 LLSRHRDELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVPVpktvVLDSADDLD-------ALAEDLGFPVVVK 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 160 ASGGGGGRGMRVVRHDK-----DLEESINMTRAEAKAAFnnDMVYMEkYLENPRHIE--VQILADGQGNAIYLaerdCSM 232
Cdd:COG3919  159 PADSVGYDELSFPGKKKvfyvdDREELLALLRRIAAAGY--ELIVQE-YIPGDDGEMrgLTAYVDRDGEVVAT----FTG 231

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138861 233 QRRHQK--------VVEEAPAPGITSEMRRYIGErcakacmeIGYRGAGTFEFLY--ENGEFYFIEMNTRI 293
Cdd:COG3919  232 RKLRHYppaggnsaARESVDDPELEEAARRLLEA--------LGYHGFANVEFKRdpRDGEYKLIEINPRF 294
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 92-322 1.49e-09

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 60.37  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   92 AEQVERSGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCVPGsdgplsdDTTKNK----AFAKRIGYPVIIKASGGGGGR 167
Cdd:PRK12815  647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG-------LTATDEeeafAFAKRIGYPVLIRPSYVIGGQ 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  168 GMRVVRHDKDLEESInmtraeAKAAFNNDMVYMEKYLENpRHIEVQILADgqGNAIYLA---ErdcsmqrrHqkvVEEA- 243
Cdd:PRK12815  720 GMAVVYDEPALEAYL------AENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiE--------H---IEQAg 779

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  244 ----------PAPGITSEMRRYIGERCAKACMEIGYRGAGTFEFLYENGEFYFIEMNTRiqVEHTV--TEMITGIDLIKE 311
Cdd:PRK12815  780 vhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPR--ASRTVpfVSKATGVPLAKL 857

                         250
                  ....*....|.
gi 488138861  312 QLRIAAGQPLS 322
Cdd:PRK12815  858 ATKVLLGKSLA 868
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 92-321 3.97e-07

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: 52.19  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  92 AEQVERSGFI----FIGPRAETIRLMGDKVSAISAMKKAGVPCVPGsdgplsdDTTKN----KAFAKRIGYPVIIKASGG 163
Cdd:COG0458   87 AVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKS-------GTATSveeaLAIAEEIGYPVIVRPSYV 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 164 GGGRGMRVVRHDKDLEESINmtraEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLaerdCSMQrrHqkvVEEA 243
Cdd:COG0458  160 LGGRGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 244 -----------PAPGITSE----MRRYiGERCAKAcmeIGYRGAGTFEFLYENGEFYFIEMNTRiqVEHTVTEM--ITGI 306
Cdd:COG0458  227 gvhsgdsicvaPPQTLSDKeyqrLRDA-TLKIARA---LGVVGLCNIQFAVDDGRVYVIEVNPR--ASRSSPFAskATGY 300

                        250
                 ....*....|....*
gi 488138861 307 DLIKEQLRIAAGQPL 321
Cdd:COG0458  301 PIAKIAAKLALGYTL 315
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 110-329 5.88e-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: 45.76  E-value: 5.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   110 IRLMGDKVSAI----------SAMKKAGVPcVPGSDGPLSDDttKNKAFAKRIGYPVIIKASGGGGGRGMRVVRHDKDLE 179
Cdd:TIGR01369  112 VEVLGTPVEAIkkaedrelfrEAMKEIGEP-VPESEIAHSVE--EALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELK 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   180 ESInmtrAEAKAAFNNDMVYMEKYLENPRHIEVQILADGQGNAIYLaerdCSMQR-----RHQK---VVeeAPAPGITSE 251
Cdd:TIGR01369  189 EIA----ERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTGdsiVV--APSQTLTDK 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861   252 MRRYIGERCAKACMEIGYRGAGTFEFLY--ENGEFYFIEMNTRIQVEHTVTEMITGIDLIKEQLRIAAGQPLsikqDEVK 329
Cdd:TIGR01369  259 EYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTL----DELK 334
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 77-292 6.22e-05

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 44.87  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  77 AVHPGY----GFLSENAD-FAEQversGFIFIGPRAETIRLMGDKVSAISAMKKAGVPCvPGSDGPLSDDTTKNKAFAKR 151
Cdd:PRK12767  72 LLIPLIdpelPLLAQNRDrFEEI----GVKVLVSSKEVIEICNDKWLTYEFLKENGIPT-PKSYLPESLEDFKAALAKGE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 152 IGYPVIIK-----ASgggggrgmrvvrhdKDLEESINMTRAEAKAAFNNDMVYMEkYLENPRhIEVQILADGQGNAIyla 226
Cdd:PRK12767 147 LQFPLFVKprdgsAS--------------IGVFKVNDKEELEFLLEYVPNLIIQE-FIEGQE-YTVDVLCDLNGEVI--- 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138861 227 erdCSMQRRHQKVVEEAPAPGITSEMRRYIgERCAKACMEIGYRGAGTFEFLYENGEFYFIEMNTR 292
Cdd:PRK12767 208 ---SIVPRKRIEVRAGETSKGVTVKDPELF-KLAERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 16-159 3.16e-04

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: 42.62  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  16 RILRACKELGIktvavhsvadrDLKHVLLADETVCIGPAPSVKSYLNIP---AIISAAeitgavaVHPGYGFlsenaDFA 92
Cdd:COG0189   18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSefdAVLPRI-------DPPFYGL-----ALL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  93 EQVERSGFIFIgPRAETIRLMGDKVSAISAMKKAGVPCvpgsdgP---LSDDTTKNKAFAKRIGYPVIIK 159
Cdd:COG0189   75 RQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------PptlVTRDPDDLRAFLEELGGPVVLK 137
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 115-291 9.40e-04

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: 40.86  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 115 DKVSAISAMKKAGVPCVPG---SDGPLSDDttknKAFAKRIGYPVIIKASGggggrgmrvvrhdkdleE--SINMT---- 185
Cdd:COG1181   95 DKALTKRVLAAAGLPTPPYvvlRRGELADL----EAIEEELGLPLFVKPAR-----------------EgsSVGVSkvkn 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861 186 RAEAKAAFNNDMVY-----MEKYLEnPRHIEVQILADGQGNA-----I------------YLAErdcsmqrrhqKVVEEA 243
Cdd:COG1181  154 AEELAAALEEAFKYddkvlVEEFID-GREVTVGVLGNGGPRAlppieIvpengfydyeakYTDG----------GTEYIC 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488138861 244 PAPgITSEMRRYIGERCAKACMEIGYRGAGTFEFLY-ENGEFYFIEMNT 291
Cdd:COG1181  223 PAR-LPEELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 123-291 9.10e-03

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: 37.30  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  123 MKKAGVPCVP-----GSDGPLSDDTTKNKAFAkRIGYPVIIKASGggggrgmrvvrhdkdLEESINMTRAEA-------- 189
Cdd:pfam07478   2 LKAAGLPVVPfvtftRADWKLNPKEWCAQVEE-ALGYPVFVKPAR---------------LGSSVGVSKVESreelqaai 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138861  190 KAAFNND-MVYMEKYLENpRHIEVQILADGQGNAIYLAER--DCSMQRRHQKVVEEA-----PApGITSEMRRYIGERCA 261
Cdd:pfam07478  66 EEAFQYDeKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELAL 143

                         170       180       190
                  ....*....|....*....|....*....|.
gi 488138861  262 KACMEIGYRGAGTFE-FLYENGEFYFIEMNT 291
Cdd:pfam07478 144 KAYKALGCRGLARVDfFLTEDGEIVLNEVNT 174
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
 244-291 9.23e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 37.88  E-value: 9.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488138861 244 PAPGITSEMRRyIGERCAKACMEIGYRGAGTFEFLYENGEFYFIEMNT 291
Cdd:PRK14571 217 PAPLNPEEERL-VKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINT 263
 
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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