NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|610505002|emb|CCO62177|]
View 

acetyl-CoA carboxylase, partial (chloroplast) [Badula decumbens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-85 3.47e-73

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: 217.85  E-value: 3.47e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002   1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:CHL00174 152 VVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYISILTSPTTGGVTASFGMLGD 231

                 ....*
gi 610505002  81 IIIAE 85
Cdd:CHL00174 232 IIIAE 236
 
Name Accession Description Interval E-value
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
1-85 3.47e-73

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 217.85  E-value: 3.47e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002   1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:CHL00174 152 VVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYISILTSPTTGGVTASFGMLGD 231

                 ....*
gi 610505002  81 IIIAE 85
Cdd:CHL00174 232 IIIAE 236
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
1-85 1.13e-53

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: 167.55  E-value: 1.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002   1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYqSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:COG0777  138 VVGEKITRAIERAIEKKLPLIIFSASGGARMQEGILSLMQMAKTSAALARL-SEAGLPYISVLTDPTTGGVTASFAMLGD 216

                 ....*
gi 610505002  81 IIIAE 85
Cdd:COG0777  217 IIIAE 221
accD TIGR00515
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase ...
1-85 5.91e-41

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: 135.31  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002    1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYqSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:TIGR00515 139 VVGEKFVRAIEKALEDNCPLIIFSASGGARMQEALLSLMQMAKTSAALAKM-SERGLPYISVLTDPTTGGVSASFAMLGD 217

                  ....*
gi 610505002   81 IIIAE 85
Cdd:TIGR00515 218 LNIAE 222
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
3-84 3.96e-08

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: 48.41  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002    3 GEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKI---SSALYDyqsnkKLFYVPILTSPTTGGvtASFG-ML 78
Cdd:pfam01039  78 GEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIfgrNSLASG-----VIPQISLIMGPCAGG--GAYLpAL 150

                  ....*.
gi 610505002   79 GDIIIA 84
Cdd:pfam01039 151 GDFVIM 156
 
Name Accession Description Interval E-value
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
1-85 3.47e-73

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 217.85  E-value: 3.47e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002   1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:CHL00174 152 VVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYISILTSPTTGGVTASFGMLGD 231

                 ....*
gi 610505002  81 IIIAE 85
Cdd:CHL00174 232 IIIAE 236
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
1-85 1.13e-53

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: 167.55  E-value: 1.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002   1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYqSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:COG0777  138 VVGEKITRAIERAIEKKLPLIIFSASGGARMQEGILSLMQMAKTSAALARL-SEAGLPYISVLTDPTTGGVTASFAMLGD 216

                 ....*
gi 610505002  81 IIIAE 85
Cdd:COG0777  217 IIIAE 221
accD TIGR00515
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; The enzyme acetyl-CoA carboxylase ...
1-85 5.91e-41

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: 135.31  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002    1 VVGEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYqSNKKLFYVPILTSPTTGGVTASFGMLGD 80
Cdd:TIGR00515 139 VVGEKFVRAIEKALEDNCPLIIFSASGGARMQEALLSLMQMAKTSAALAKM-SERGLPYISVLTDPTTGGVSASFAMLGD 217

                  ....*
gi 610505002   81 IIIAE 85
Cdd:TIGR00515 218 LNIAE 222
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
3-84 3.96e-08

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: 48.41  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610505002    3 GEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKI---SSALYDyqsnkKLFYVPILTSPTTGGvtASFG-ML 78
Cdd:pfam01039  78 GEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIfgrNSLASG-----VIPQISLIMGPCAGG--GAYLpAL 150

                  ....*.
gi 610505002   79 GDIIIA 84
Cdd:pfam01039 151 GDFVIM 156
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
3-44 9.57e-06

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 41.55  E-value: 9.57e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 610505002   3 GEKITRLIEYATKKFLPLILVCASGGARMQEGSLSLMQMAKI 44
Cdd:COG4799  103 AKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRI 144
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH