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Conserved domains on  [gi|2255892465|ref|WP_251889785|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxyl carrier protein subunit [Klebsiella]

Protein Classification

acetyl-CoA carboxylase biotin carboxyl carrier protein( domain architecture ID 11423502)

acetyl-CoA carboxylase biotin carboxyl carrier protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA

CATH:  2.40.50.100
Gene Ontology:  GO:0003989|GO:0006633|GO:0009317
PubMed:  1370469
SCOP:  4002909
TCDB:  3.B.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 15-130 8.10e-15

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


:

Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 66.46  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892465  15 LAQKMHNAGLRELEWRGADWSVRLRYPSGKTMAEPPPLPPLAAETRPLS-------------VCSPMPGRLLLSHPSHGE 81
Cdd:COG0511     1 LIELLEESGLTELEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAPAaaaaaaaasgggaVKSPMVGTFYRAPSPGAK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2255892465  82 AFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYG 130
Cdd:COG0511    81 PFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYG 129
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 15-130 8.10e-15

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


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 66.46  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892465  15 LAQKMHNAGLRELEWRGADWSVRLRYPSGKTMAEPPPLPPLAAETRPLS-------------VCSPMPGRLLLSHPSHGE 81
Cdd:COG0511     1 LIELLEESGLTELEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAPAaaaaaaaasgggaVKSPMVGTFYRAPSPGAK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2255892465  82 AFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYG 130
Cdd:COG0511    81 PFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYG 129
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 64-136 2.43e-11

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 55.50  E-value: 2.43e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255892465  64 VCSPMPGRLLlshpshgEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALL 136
Cdd:cd06850     2 VTAPMPGTVV-------KVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 66-136 1.97e-08

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 48.36  E-value: 1.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255892465  66 SPMPGrlLLSHPSHGEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALL 136
Cdd:pfam00364   5 SPMIG--ESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 64-138 4.10e-05

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 42.14  E-value: 4.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255892465  64 VCSPMPGRLLlshpshgEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALLLP 138
Cdd:PRK09282  525 VTSPMPGTVV-------KVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 15-130 8.10e-15

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


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 66.46  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892465  15 LAQKMHNAGLRELEWRGADWSVRLRYPSGKTMAEPPPLPPLAAETRPLS-------------VCSPMPGRLLLSHPSHGE 81
Cdd:COG0511     1 LIELLEESGLTELEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAPAaaaaaaaasgggaVKSPMVGTFYRAPSPGAK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2255892465  82 AFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYG 130
Cdd:COG0511    81 PFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYG 129
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 64-136 2.43e-11

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 55.50  E-value: 2.43e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255892465  64 VCSPMPGRLLlshpshgEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALL 136
Cdd:cd06850     2 VTAPMPGTVV-------KVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 66-136 1.97e-08

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 48.36  E-value: 1.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255892465  66 SPMPGrlLLSHPSHGEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALL 136
Cdd:pfam00364   5 SPMIG--ESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 64-138 4.10e-05

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 42.14  E-value: 4.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255892465  64 VCSPMPGRLLlshpshgEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALLLP 138
Cdd:PRK09282  525 VTSPMPGTVV-------KVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 83-136 2.39e-04

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 37.35  E-value: 2.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2255892465  83 FVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALL 136
Cdd:COG0508    23 LVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 61-130 1.15e-03

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: 37.75  E-value: 1.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255892465   61 PLSVCSPMPGRLLlshpshgEAFVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYG 130
Cdd:COG1038   1076 PGHIGAPMPGTVV-------KVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
66-136 1.48e-03

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 35.37  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255892465  66 SPMPGrLLLSHPSHGEA-FVSEGQHVAPNDILALLQVGPLYLPVRSPVAGTLKNLVAPAGSRLEYGSEIALL 136
Cdd:PRK07051    8 SPLPG-TFYRRPSPDAPpYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 81-144 1.73e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 37.49  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255892465  81 EAFVSEGQHVAPNDIL-------ALLQVgplylPvrSPVAGTLKNLVAPAGSRLEYGSEIALLLPTDAASA 144
Cdd:PRK11855   20 EWLVKEGDTVEEDQPLvtvetdkATMEI-----P--SPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAAAA 83
 
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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