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Conserved domains on  [gi|164453500|gb|ABY57509|]
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AccD, partial (chloroplast) [Triticum monococcum]

Protein Classification

Clp protease/crotonase-like domain-containing protein( domain architecture ID 581041)

Clp protease/crotonase-like domain-containing protein similar to Oryza sativa enoyl-CoA delta isomerase which plays a role in fatty acid metabolism, which involves stabilization of an enolate anion intermediate derived from an acyl-CoA substrate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
crotonase-like super family cl23717
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
1-114 4.79e-101

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


The actual alignment was detected with superfamily member CHL00174:

Pssm-ID: 474030 [Multi-domain]  Cd Length: 296  Bit Score: 289.88  E-value: 4.79e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500   1 FLPLILVCASGGARMQEGSVSLMQMAKISSALYDYQSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKR 80
Cdd:CHL00174 168 SLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYISILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKR 247
                         90       100       110
                 ....*....|....*....|....*....|....
gi 164453500  81 VIEQTLNTTVPEGSQVAEYLFDKGLFDLIVPRNP 114
Cdd:CHL00174 248 VIEQTLNKTVPEGSQAAEYLFDKGLFDLIVPRNL 281
 
Name Accession Description Interval E-value
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
1-114 4.79e-101

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 289.88  E-value: 4.79e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500   1 FLPLILVCASGGARMQEGSVSLMQMAKISSALYDYQSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKR 80
Cdd:CHL00174 168 SLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYISILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKR 247
                         90       100       110
                 ....*....|....*....|....*....|....
gi 164453500  81 VIEQTLNTTVPEGSQVAEYLFDKGLFDLIVPRNP 114
Cdd:CHL00174 248 VIEQTLNKTVPEGSQAAEYLFDKGLFDLIVPRNL 281
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
2-112 8.18e-68

Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440540 [Multi-domain]  Cd Length: 280  Bit Score: 204.91  E-value: 8.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500   2 LPLILVCASGGARMQEGSVSLMQMAKISSALYDYqSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRV 81
Cdd:COG0777  155 LPLIIFSASGGARMQEGILSLMQMAKTSAALARL-SEAGLPYISVLTDPTTGGVTASFAMLGDIIIAEPGALIGFAGPRV 233
                         90       100       110
                 ....*....|....*....|....*....|.
gi 164453500  82 IEQTLNTTVPEGSQVAEYLFDKGLFDLIVPR 112
Cdd:COG0777  234 IEQTIREKLPEGFQRAEFLLEHGFIDMIVHR 264
accD TIGR00515
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase ...
2-112 2.29e-54

acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the beta chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129606 [Multi-domain]  Cd Length: 285  Bit Score: 171.14  E-value: 2.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500    2 LPLILVCASGGARMQEGSVSLMQMAKISSALYDYqSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRV 81
Cdd:TIGR00515 156 CPLIIFSASGGARMQEALLSLMQMAKTSAALAKM-SERGLPYISVLTDPTTGGVSASFAMLGDLNIAEPKALIGFAGPRV 234
                          90       100       110
                  ....*....|....*....|....*....|.
gi 164453500   82 IEQTLNTTVPEGSQVAEYLFDKGLFDLIVPR 112
Cdd:TIGR00515 235 IEQTVREKLPEGFQTSEFLLEHGAIDMIVHR 265
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
2-90 9.39e-07

Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.


Pssm-ID: 426008 [Multi-domain]  Cd Length: 491  Bit Score: 45.71  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500    2 LPLILVCASGGARMQEGSVSLMQMAKI---SSALYDyqsnkKLFYVAILTSPTTGGvtASFG-MLGDIIIA-EPNAYIAF 76
Cdd:pfam01039  93 LPLIGINDSGGARIQEGVENLRGSGKIfgrNSLASG-----VIPQISLIMGPCAGG--GAYLpALGDFVIMvEGTSPMFL 165
                          90
                  ....*....|....
gi 164453500   77 AGKRVIEQTLNTTV 90
Cdd:pfam01039 166 TGPPVIKKVTGEEV 179
 
Name Accession Description Interval E-value
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
1-114 4.79e-101

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 289.88  E-value: 4.79e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500   1 FLPLILVCASGGARMQEGSVSLMQMAKISSALYDYQSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKR 80
Cdd:CHL00174 168 SLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYISILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKR 247
                         90       100       110
                 ....*....|....*....|....*....|....
gi 164453500  81 VIEQTLNTTVPEGSQVAEYLFDKGLFDLIVPRNP 114
Cdd:CHL00174 248 VIEQTLNKTVPEGSQAAEYLFDKGLFDLIVPRNL 281
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
2-112 8.18e-68

Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440540 [Multi-domain]  Cd Length: 280  Bit Score: 204.91  E-value: 8.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500   2 LPLILVCASGGARMQEGSVSLMQMAKISSALYDYqSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRV 81
Cdd:COG0777  155 LPLIIFSASGGARMQEGILSLMQMAKTSAALARL-SEAGLPYISVLTDPTTGGVTASFAMLGDIIIAEPGALIGFAGPRV 233
                         90       100       110
                 ....*....|....*....|....*....|.
gi 164453500  82 IEQTLNTTVPEGSQVAEYLFDKGLFDLIVPR 112
Cdd:COG0777  234 IEQTIREKLPEGFQRAEFLLEHGFIDMIVHR 264
accD TIGR00515
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase ...
2-112 2.29e-54

acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the beta chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129606 [Multi-domain]  Cd Length: 285  Bit Score: 171.14  E-value: 2.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500    2 LPLILVCASGGARMQEGSVSLMQMAKISSALYDYqSNKKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRV 81
Cdd:TIGR00515 156 CPLIIFSASGGARMQEALLSLMQMAKTSAALAKM-SERGLPYISVLTDPTTGGVSASFAMLGDLNIAEPKALIGFAGPRV 234
                          90       100       110
                  ....*....|....*....|....*....|.
gi 164453500   82 IEQTLNTTVPEGSQVAEYLFDKGLFDLIVPR 112
Cdd:TIGR00515 235 IEQTVREKLPEGFQTSEFLLEHGAIDMIVHR 265
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
2-90 9.39e-07

Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.


Pssm-ID: 426008 [Multi-domain]  Cd Length: 491  Bit Score: 45.71  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500    2 LPLILVCASGGARMQEGSVSLMQMAKI---SSALYDyqsnkKLFYVAILTSPTTGGvtASFG-MLGDIIIA-EPNAYIAF 76
Cdd:pfam01039  93 LPLIGINDSGGARIQEGVENLRGSGKIfgrNSLASG-----VIPQISLIMGPCAGG--GAYLpALGDFVIMvEGTSPMFL 165
                          90
                  ....*....|....
gi 164453500   77 AGKRVIEQTLNTTV 90
Cdd:pfam01039 166 TGPPVIKKVTGEEV 179
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
2-83 1.17e-04

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 39.63  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164453500   2 LPLILVCASGGARMQEGSVSLMQMAKIssalydyqsnkklFY-----------VAILTSPTTGGVTASFGMlGDIIIA-E 69
Cdd:COG4799  118 LPVIYLVDSGGARLQEGVESFAGYGRI-------------FYrnarssggipqISVIMGPCAAGGAYSPAL-SDFVIMvK 183
                         90
                 ....*....|....
gi 164453500  70 PNAYIAFAGKRVIE 83
Cdd:COG4799  184 GTSQMFLGGPPVVK 197
 
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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