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Conserved domains on  [gi|491115384|ref|WP_004973841|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxylase subunit [Acinetobacter]

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
 1-446 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


:

Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 793.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVdDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAkNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDLiLQDKNFCKQAMDIHYLEKHLLKQ 446
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRL-LNDPNFQAGDYNIHYLEKKLALQ 448
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-446 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 793.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVdDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAkNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDLiLQDKNFCKQAMDIHYLEKHLLKQ 446
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRL-LNDPNFQAGDYNIHYLEKKLALQ 448
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-455 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 760.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKaa 159
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVqDAEEALAIAEEIGYPVLIKas 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 aggggrgMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:COG4770  161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLF-EDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPArGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDlILQDKNFCKQAMDIHYLEKHLLKQLAGNEEEKA 455
Cdd:COG4770  401 ARMRRALAEFVIEGVKTNIPFLRA-LLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-443 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: 647.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVeDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNgEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIkTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 491115384  398 ARMRQALDETILTGIKTNIPLHKdLILQDKNFCKQAMDIHYLEKHL 443
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQ-RILEDENFQHGGTNIHYLEKKL 445
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 116-320 1.38e-78

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: 242.98  E-value: 1.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  116 KVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDD 194
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVeTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  195 TVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLEEAPAPNLPEQARADILEACVNACKLMQYRGAGTFE 274
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491115384  275 FLFE--DDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLGLD 320
Cdd:pfam02786 162 FALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 334-440 1.14e-57

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: 185.31  E-value: 1.14e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   334 ECRINAEDP-TTFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSIARMRQALDETILTGI 412
Cdd:smart00878   1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*...
gi 491115384   413 KTNIPLHKDlILQDKNFCKQAMDIHYLE 440
Cdd:smart00878  81 KTNIPFLRA-LLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-446 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 793.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVdDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAkNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDLiLQDKNFCKQAMDIHYLEKHLLKQ 446
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRL-LNDPNFQAGDYNIHYLEKKLALQ 448
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-455 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 760.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKaa 159
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVqDAEEALAIAEEIGYPVLIKas 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 aggggrgMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:COG4770  161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLF-EDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPArGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDlILQDKNFCKQAMDIHYLEKHLLKQLAGNEEEKA 455
Cdd:COG4770  401 ARMRRALAEFVIEGVKTNIPFLRA-LLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 651.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK06111   1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:PRK06111  81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLeDAEEAIAIARQIGYPVMLKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDDE-YFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPTTFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSIA 398
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAIS 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 491115384 399 RMRQALDETILTGIKTNIPLHKDlILQDKNFCKQAMDIHYLEKHLLK 445
Cdd:PRK06111 401 RLHDALEELKVEGIKTNIPLLLQ-VLEDPVFKAGGYTTGFLTKQLVK 446
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-443 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: 647.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVeDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNgEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIkTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 491115384  398 ARMRQALDETILTGIKTNIPLHKdLILQDKNFCKQAMDIHYLEKHL 443
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQ-RILEDENFQHGGTNIHYLEKKL 445
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-442 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 638.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK08654   1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAVTPHNALAE-AKEIGFPLIVKAA 159
Cdd:PRK08654  81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEiAEEIGYPVIIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLGL 319
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 320 DIEQDQVEIRGHAIECRINAEDP-TTFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSIA 398
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIA 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 491115384 399 RMRQALDETILTGIKTNIPLHKdLILQDKNFCKQAMDIHYLEKH 442
Cdd:PRK08654 401 RMRRALYEYVIVGVKTNIPFHK-AVMENENFVRGNLHTHFIEEE 443
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: 588.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK05586   1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:PRK05586  81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIeNEEEALEIAKEIGYPVMVKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLF-EDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPTT-FVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:PRK05586 321 LSIKQEDIKINGHSIECRINAEDPKNgFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKdLILQDKNFCKQAMDIHYLEKHLLK 445
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQF-IILEDEEFIKGTYDTSFIEKKLVD 447
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-429 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: 565.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHlRF-CDEAVCIGPGASS-ESYLNIPAIITAAEITGADAI 78
Cdd:COG1038     3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLH-RFkADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   79 HPGYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAVT-PHNALAEAKEIGFPLIVK 157
Cdd:COG1038    82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDdLEEALAFAEEIGYPVMLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  158 AAAGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKV 237
Cdd:COG1038   162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  238 LEEAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLF-EDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAG 316
Cdd:COG1038   242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  317 LGLDIE------QDQVEIRGHAIECRINAEDPTT-FVPSPGKIEHFYAPGGAGVRVDS-HIYEGYSIPPYYDSMIAKLIV 388
Cdd:COG1038   322 YSLDDPeigipsQEDIRLNGYAIQCRITTEDPANnFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVKVTA 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 491115384  389 HGKDRETSIARMRQALDETILTGIKTNIP-LHKdlILQDKNF 429
Cdd:COG1038   402 WGRTFEEAIRKMRRALREFRIRGVKTNIPfLEN--VLNHPDF 441
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-429 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 562.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIG-PGASSESYLNIPAIITAAEITGADAIH 79
Cdd:PRK12999    4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGeGKHPVRAYLDIDEIIRVAKQAGVDAIH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   80 PGYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAVT-PHNALAEAKEIGFPLIVKA 158
Cdd:PRK12999   84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDdIEEALEFAEEIGYPIMLKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  159 AAGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVL 238
Cdd:PRK12999  164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  239 EEAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLF-EDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGL 317
Cdd:PRK12999  244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  318 GLD------IEQDQVEIRGHAIECRINAEDPTT-FVPSPGKIEHFYAPGGAGVRVDS-HIYEGYSIPPYYDSMIAKLIVH 389
Cdd:PRK12999  324 TLHdleigiPSQEDIRLRGYAIQCRITTEDPANnFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTAW 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 491115384  390 GKDRETSIARMRQALDETILTGIKTNIPLHKDlILQDKNF 429
Cdd:PRK12999  404 GRTFEQAVARMRRALREFRIRGVKTNIPFLEN-VLKHPDF 442
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
2-442 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 559.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   2 LQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHPG 81
Cdd:PRK08462   4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  82 YGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAVTPHNALAE-AKEIGFPLIVKAAA 160
Cdd:PRK08462  84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKiAKEIGYPVILKAAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 161 GGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLEE 240
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 241 APAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLGL 319
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 320 dIEQDQVEIRGHAIECRINAEDPTTFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSIAR 399
Cdd:PRK08462 324 -PSQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAK 402

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 491115384 400 MRQALDETILTGIKTNIPLHKDLiLQDKNFCKQAMDIHYLEKH 442
Cdd:PRK08462 403 MKRALKEFKVEGIKTTIPFHLEM-MENADFINNKYDTKYLEEH 444
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 2-440 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 554.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   2 LQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHPG 81
Cdd:PRK12833   5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  82 YGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAVTP-HNALAEAKEIGFPLIVKAAA 160
Cdd:PRK12833  85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASlDAALEVAARIGYPLMIKAAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 161 GGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNgHAIHLYDRDCSLQRRHQKVLEE 240
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 241 APAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFED--DEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLrDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDLiLQDKNFCKQAMDIHYLE 440
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRAL-LADADVRAGRFHTNFLE 445
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-442 7.10e-180

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 511.18  E-value: 7.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGaSSESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK07178   1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD-PLAGYLNPRRLVNLAVETGCDALHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:PRK07178  80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLaDLDEALAEAERIGYPVMLKAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFE-DDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 319 LDIEQDQVEIRGHAIECRINAEDPTT-FVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSI 397
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNdFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEAL 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 491115384 398 ARMRQALDETILTGIKTNIPLHKDlILQDKNFCKQAMDIHYLEKH 442
Cdd:PRK07178 400 DRGRRALDDMRVQGVKTTIPYYQE-ILRNPEFRSGQFNTSFVESH 443
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-443 1.35e-160

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 462.36  E-value: 1.35e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   1 MLQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASsESYLNIPAIITAAEITGADAIHP 80
Cdd:PRK08463   1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPG-------SAHAVTPHnalaeAKEIGFP 153
Cdd:PRK08463  80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGteklnseSMEEIKIF-----ARKIGYP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 154 LIVKAAAGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRR 233
Cdd:PRK08463 155 VILKASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRR 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 234 HQKVLEEAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFED-DEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLR 312
Cdd:PRK08463 235 HQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 313 IAAGLGLDIEQDQVEIRGHAIECRINAEDP-TTFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGK 391
Cdd:PRK08463 315 IAAGEILDLEQSDIKPRGFAIEARITAENVwKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKAT 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491115384 392 DRETSIARMRQALDETILTGIKTNIPLHKDlILQDKNFCKQAMDIHYLEKHL 443
Cdd:PRK08463 395 SYDLAVNKLERALKEFVIDGIRTTIPFLIA-ITKTREFRRGYFDTSYIETHM 445
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 4-442 3.09e-153

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: 464.30  E-value: 3.09e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384     4 KVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPG---ASSESYLNIPAIITAAEITGADAIHP 80
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdlGPIEAYLSIDEIIRVAKLNGVDAIHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    81 GYGFLAENAEFAEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAA 159
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPeTMEEVLDFAAAIGYPVIIKAS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   160 AGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLE 239
Cdd:TIGR01235  161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   240 EAPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLF-EDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLG 318
Cdd:TIGR01235  241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   319 LDI------EQDQVEIRGHAIECRINAEDPT-TFVPSPGKIEHFYAPGGAGVRVDS-HIYEGYSIPPYYDSMIAKLIVHG 390
Cdd:TIGR01235  321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPAnNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAWA 400

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 491115384   391 KDRETSIARMRQALDETILTGIKTNIPLHKDLILQDKnFCKQAMDIHYLEKH 442
Cdd:TIGR01235  401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPK-FLDGSYDTRFIDTT 451
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 116-320 1.38e-78

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: 242.98  E-value: 1.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  116 KVSAITAMRKAGVPTVPGSAHAV-TPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDD 194
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVeTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  195 TVYMERFLQKPRHVEVQVLADGNGHAIHLYDRDCSLQRRHQKVLEEAPAPNLPEQARADILEACVNACKLMQYRGAGTFE 274
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491115384  275 FLFE--DDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAGLGLD 320
Cdd:pfam02786 162 FALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 62-317 3.05e-62

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: 202.80  E-value: 3.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  62 NIPAII-TAAEI---TGADAIhpgygfLAENAE----FAEIVESSGFIfiGPRPEHIRLMGNKVSAITAMRKAGVPtVPG 133
Cdd:COG0439    1 DIDAIIaAAAELareTGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 134 SAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVQAAQRDAEMWFGDDTVYMERFLQKpRHVEVQVL 213
Cdd:COG0439   72 FALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 214 ADgNGHAIHlydrdCSLQRRHQK---VLE---EAPAPnLPEQARADILEACVNACKLMQY-RGAGTFEFLF-EDDEYFFI 285
Cdd:COG0439  151 VR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLI 223

                        250       260       270
                 ....*....|....*....|....*....|....
gi 491115384 286 EMNTRVQVEH--PVTEMVTGIDIIEQQLRIAAGL 317
Cdd:COG0439  224 EINARLGGEHipPLTELATGVDLVREQIRLALGE 257
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-109 1.45e-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: 1.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    2 LQKVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAVCIGPGASSESYLNIPAIITAAEITGADAIHPG 81
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 491115384   82 YGFLAENAEFAEIVESSGFIFIGPRPEH 109
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 334-440 1.14e-57

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: 185.31  E-value: 1.14e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   334 ECRINAEDP-TTFVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSIARMRQALDETILTGI 412
Cdd:smart00878   1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*...
gi 491115384   413 KTNIPLHKDlILQDKNFCKQAMDIHYLE 440
Cdd:smart00878  81 KTNIPFLRA-LLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 334-441 6.66e-56

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: 180.77  E-value: 6.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  334 ECRINAEDPTT-FVPSPGKIEHFYAPGGAGVRVDSHIYEGYSIPPYYDSMIAKLIVHGKDRETSIARMRQALDETILTGI 412
Cdd:pfam02785   1 EARIYAEDPDNnFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80

                          90       100
                  ....*....|....*....|....*....
gi 491115384  413 KTNIPLHKDlILQDKNFCKQAMDIHYLEK 441
Cdd:pfam02785  81 KTNIPFLRA-ILEHPDFRAGEVDTGFLEE 108
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
4-291 2.01e-11

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 65.33  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   4 KVLIANRGEIALRITRACKTLGIKTVGIYSDADKDLMHLRFCDEAV-CIGPGASSESYLNipAIITAAEITGADAIHPGY 82
Cdd:COG3919    7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvVPDPGDDPEAFVD--ALLELAERHGPDVLIPTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  83 ----GFLAEN-AEFAEivessGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPtVPGSAHAVTPHNALAEAKEIGFPLIVK 157
Cdd:COG3919   85 deyvELLSRHrDELEE-----HYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTVVLDSADDLDALAEDLGFPVVVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 158 -----AAAGGGGRGMRIVERVDTL--LESVQAAQRDAEMWF-------GDDTvyMERFlqkprhveVQVLADGNGHAIHL 223
Cdd:COG3919  159 padsvGYDELSFPGKKKVFYVDDReeLLALLRRIAAAGYELivqeyipGDDG--EMRG--------LTAYVDRDGEVVAT 228

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491115384 224 ydrdCSLQRRHQK--------VLEEAPAPNLPEQARAdILEAcvnacklMQYRGAGTFEFLF--EDDEYFFIEMNTRV 291
Cdd:COG3919  229 ----FTGRKLRHYppaggnsaARESVDDPELEEAARR-LLEA-------LGYHGFANVEFKRdpRDGEYKLIEINPRF 294
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 92-316 1.35e-09

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


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 60.40  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384    92 AEIVESSGFIFIGPRPEHIRLMGNKVSAITAMRKAGVPTVPGSAhAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVE 171
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKT-ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVY 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   172 RVDTLLESVQAAQRDAEmwfgDDTVYMERFLQKPRHVEVQVLADGN---GHAI---------HLYDRDCSLqrrhqkvle 239
Cdd:TIGR01369  725 NEEELRRYLEEAVAVSP----EHPVLIDKYLEDAVEVDVDAVSDGEevlIPGImehieeagvHSGDSTCVL--------- 791

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491115384   240 eaPAPNLPEQARADILEACVNACKLMQYRGAGTFEFLFEDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAG 316
Cdd:TIGR01369  792 --PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLG 866
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 108-291 2.46e-08

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: 56.04  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 108 EHIRLMGNKVSAI----------TAMRKAGVPtVPGSAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLL 177
Cdd:COG0458   97 EGVKILGTSPDAIdlaedrelfkELLDKLGIP-QPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELE 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 178 ESVQAAQRDAemwfGDDTVYMERFLQKPRHVEVQVLADGNGHAIHLydrdCSLQrrHqkvLEEA-----------PAPNL 246
Cdd:COG0458  176 EYLERALKVS----PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTL 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491115384 247 PEQARADILEAcvnACKLMQ---YRGAGTFEFLFEDDEYFFIEMNTRV 291
Cdd:COG0458  243 SDKEYQRLRDA---TLKIARalgVVGLCNIQFAVDDGRVYVIEVNPRA 287
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 123-316 7.69e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 54.98  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  123 MRKAGVPTVPGsAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVqaaqrdAEMWFGDDTVYMERFL 202
Cdd:PRK12815  678 LDELGLPHVPG-LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYL------AENASQLYPILIDQFI 750

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  203 QKpRHVEVQVLADGNG--------H----AIHLYDRDCSLqrrhqkvleeaPAPNLPEQARADILEACVNACKLMQYRGA 270
Cdd:PRK12815  751 DG-KEYEVDAISDGEDvtipgiieHieqaGVHSGDSIAVL-----------PPQSLSEEQQEKIRDYAIKIAKKLGFRGI 818

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 491115384  271 GTFEFLFEDDEYFFIEMNTRVQVEHPVTEMVTGIDIIEQQLRIAAG 316
Cdd:PRK12815  819 MNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 115-289 5.70e-07

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: 50.88  E-value: 5.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 115 NKVSAITAMRKAGVPTVPG-SAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVQAAQRdaemwfGD 193
Cdd:COG1181   95 DKALTKRVLAAAGLPTPPYvVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFK------YD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 194 DTVYMERFLqKPRHVEVQVLADGNGHA-----I----HLYDRDCSLQRrhQKVLEEAPAPnLPEQARADILEACVNACKL 264
Cdd:COG1181  169 DKVLVEEFI-DGREVTVGVLGNGGPRAlppieIvpenGFYDYEAKYTD--GGTEYICPAR-LPEELEERIQELALKAFRA 244

                        170       180
                 ....*....|....*....|....*.
gi 491115384 265 MQYRGAGTFEFLF-EDDEYFFIEMNT 289
Cdd:COG1181  245 LGCRGYARVDFRLdEDGEPYLLEVNT 270
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 29-309 3.15e-06

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: 48.78  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  29 VGIYSDADKDLMHLRFCDEA-------VCIGPGASSESYLNIPAIITAAEITGADAI-----HPGYGFlaenaEFAEIVE 96
Cdd:COG0189    4 IAILTDPPDKDSTKALIEAAqrrghevEVIDPDDLTLDLGRAPELYRGEDLSEFDAVlpridPPFYGL-----ALLRQLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  97 SSGFIFIgPRPEHIRLMGNKVSAITAMRKAGVPTVPgSAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTL 176
Cdd:COG0189   79 AAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP-TLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 177 LESVQAAQRDaemwfGDDTVYMERFLQKPRHVEVQVLADGnGHAIHLYDRDCSLQ--RRHQKVLEEAPAPNLPEQARadi 254
Cdd:COG0189  157 ESILEALTEL-----GSEPVLVQEFIPEEDGRDIRVLVVG-GEPVAAIRRIPAEGefRTNLARGGRAEPVELTDEER--- 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491115384 255 lEACVNACKLMQYRGAGtFEFLFEDDEYFFIEMNTRVQVEHpvTEMVTGIDIIEQ 309
Cdd:COG0189  228 -ELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNVTPGFRG--LERATGVDIAEA 278
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 63-320 6.60e-06

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 48.69  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  63 IPAIITAAEITGADAIHpgyGFLAENAEFAEIVESSGFiFI-------------GPRPEHIRLMGNKVSAITAMRKAGVP 129
Cdd:PRK02186  46 IRVVTISADTSDPDRIH---RFVSSLDGVAGIMSSSEY-FIevasevarrlglpAANTEAIRTCRDKKRLARTLRDHGID 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 130 tVPgSAHAVTPHNALAEA-KEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVQAAQRdaemwFGDDTVYMERFLQKPRHv 208
Cdd:PRK02186 122 -VP-RTHALALRAVALDAlDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRR-----AGTRAALVQAYVEGDEY- 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 209 EVQVLADGNGHAI------HLYDRDCSLQRRHqkvleEAPAPnLPEQARADILEACVNACKLMQYR-GAGTFEFLFEDDE 281
Cdd:PRK02186 194 SVETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAP-LSAPQRERIVRTVLRALDAVGYAfGPAHTELRVRGDT 267

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 491115384 282 YFFIEMNTR-------VQVEHpvtemVTGIDIIEQQLRIAAGLGLD 320
Cdd:PRK02186 268 VVIIEINPRlaggmipVLLEE-----AFGVDLLDHVIDLHLGVAAF 308
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 123-289 1.33e-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: 45.77  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  123 MRKAGVPTVPgsAHAVTPHN--------ALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLlesvQAAQRDAEMWfgDD 194
Cdd:pfam07478   2 LKAAGLPVVP--FVTFTRADwklnpkewCAQVEEALGYPVFVKPARLGSSVGVSKVESREEL----QAAIEEAFQY--DE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  195 TVYMERFLqKPRHVEVQVLADGNGHAIHL---------YDRDCslqrrhqKVLEEA-----PAPnLPEQARADILEACVN 260
Cdd:pfam07478  74 KVLVEEGI-EGREIECAVLGNEDPEVSPVgeivpsggfYDYEA-------KYIDDSaqivvPAD-LEEEQEEQIQELALK 144

                         170       180       190
                  ....*....|....*....|....*....|
gi 491115384  261 ACKLMQYRGAGTFE-FLFEDDEYFFIEMNT 289
Cdd:pfam07478 145 AYKALGCRGLARVDfFLTEDGEIVLNEVNT 174
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 92-314 2.97e-05

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 45.42  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384   92 AEIVESSGFIFIGPrPEHIRLMGNKVSAITAMRKAGVPTvPGSAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIVE 171
Cdd:TIGR00768  66 LRYLESLGVPVINS-SDAILNAGDKFLSHQLLAKAGIPL-PRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLAR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  172 RVD---TLLESVQAAQRDAEmwfgddTVYMERFLQKPRHVEVQVLADGNG--HAIH-LYDRD----CSLQRRhqkvleEA 241
Cdd:TIGR00768 144 DRQaaeSLLEHFEQLNGPQN------LFLVQEYIKKPGGRDIRVFVVGDEvvAAIYrITSGHwrsnLARGGK------AE 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491115384  242 PAPNLPEQAradilEACVNACKLMQYRGAGTfEFLFEDDEYFFIEMNTRVQVEHpvTEMVTGIDIIEQQLRIA 314
Cdd:TIGR00768 212 PCSLTEEIE-----ELAIKAAKALGLDVAGV-DLLESEDGLLVNEVNANPEFKN--SVKTTGVNIAGKLLDYI 276
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 42-290 4.70e-05

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 45.26  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  42 LRFCDEAVcIGPGASSESYlnIPAIITAAEITGADAIHPGY----GFLAENA-EFAEIvessGFIFIGPRPEHIRLMGNK 116
Cdd:PRK12767  40 LYFADKFY-VVPKVTDPNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQNRdRFEEI----GVKVLVSSKEVIEICNDK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 117 VSAITAMRKAGVPTvPGSAHAVTPHNALA--EAKEIGFPLIVKAAAGGGGRGMRIVERVDTLlesvqaaqrDAEMWFGDD 194
Cdd:PRK12767 113 WLTYEFLKENGIPT-PKSYLPESLEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEEL---------EFLLEYVPN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 195 TVYMErFLQKPRhVEVQVLADGNGHAIHLYDRdcslqRRHQKVLEEApapnlpEQARA----DILEACVNACKLMQYRGA 270
Cdd:PRK12767 183 LIIQE-FIEGQE-YTVDVLCDLNGEVISIVPR-----KRIEVRAGET------SKGVTvkdpELFKLAERLAEALGARGP 249

                        250       260
                 ....*....|....*....|
gi 491115384 271 GTFEFLFEDDEYFFIEMNTR 290
Cdd:PRK12767 250 LNIQCFVTDGEPYLFEINPR 269
PLN02735 PLN02735
carbamoyl-phosphate synthase
 132-290 4.75e-05

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 45.92  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  132 PGSAHAVTPHNALAEAKEIGFPLIVKAAAGGGGRGMRIV---ERVDTLLESvqAAQRDAEMwfgddTVYMERFLQKPRHV 208
Cdd:PLN02735  718 PKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVysdDKLKTYLET--AVEVDPER-----PVLVDKYLSDATEI 790

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384  209 EVQVLADGNGH-------------AIHLYDRDCSLqrrhqkvleeaPAPNLPEQARADI------LEACVNACKLMQYRG 269
Cdd:PLN02735  791 DVDALADSEGNvviggimehieqaGVHSGDSACSL-----------PTQTIPSSCLATIrdwttkLAKRLNVCGLMNCQY 859

                         170       180
                  ....*....|....*....|.
gi 491115384  270 AGTfeflfEDDEYFFIEMNTR 290
Cdd:PLN02735  860 AIT-----PSGEVYIIEANPR 875
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 118-289 2.39e-04

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 42.79  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 118 SAItAMRK---------AGVPTVPGSAhaVTPH-NALAEAKEIGFPLIVKAAAGGGGRGMRIVERVDTLLESVQAAqrda 187
Cdd:PRK01372  93 SAL-AMDKlrtklvwqaAGLPTPPWIV--LTREeDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELA---- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491115384 188 emWFGDDTVYMERFLqKPRHVEVQVLadgNGHAI---------HLYDRDcslqrrhQKVLEEA-----PAPnLPEQARAD 253
Cdd:PRK01372 166 --FKYDDEVLVEKYI-KGRELTVAVL---GGKALpvieivpagEFYDYE-------AKYLAGGtqyicPAG-LPAEIEAE 231

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491115384 254 ILEACVNACKLMQYRGAGTFEFLFEDD-EYFFIEMNT 289
Cdd:PRK01372 232 LQELALKAYRALGCRGWGRVDFMLDEDgKPYLLEVNT 268
carB PRK05294
carbamoyl-phosphate synthase large subunit;
110-156 1.72e-03

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 40.85  E-value: 1.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 491115384  110 IRLMGNKVSAI----------TAMRKAGVPtVPGSAHAVTPHNALAEAKEIGFPLIV 156
Cdd:PRK05294  113 VELIGAKLEAIdkaedrelfkEAMKKIGLP-VPRSGIAHSMEEALEVAEEIGYPVII 168
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 110-157 2.68e-03

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: 40.37  E-value: 2.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 491115384   110 IRLMGNKVSAI----------TAMRKAGVPtVPGSAHAVTPHNALAEAKEIGFPLIVK 157
Cdd:TIGR01369  112 VEVLGTPVEAIkkaedrelfrEAMKEIGEP-VPESEIAHSVEEALAAAKEIGYPVIVR 168
 
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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