Q8X9B6 · ACCC_ECO57
- ProteinBiotin carboxylase
- GeneaccC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids449 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
This 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.
Catalytic activity
- ATP + hydrogencarbonate + N6-biotinyl-L-lysyl-[protein] = ADP + H+ + N6-carboxybiotinyl-L-lysyl-[protein] + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 magnesium or manganese ions per subunit.
Pathway
Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 165-166 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 201-204 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EKYL | ||||||
Binding site | 209 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 236 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 238 | hydrogencarbonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 276 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 276 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 276 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 288 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 288 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 288 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 288 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 288 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 290 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 290 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 292 | |||||
Sequence: R | ||||||
Binding site | 292 | hydrogencarbonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 295 | hydrogencarbonate (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 338 | biotin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 338 | hydrogencarbonate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | acetyl-CoA carboxylase activity | |
Molecular Function | ATP binding | |
Molecular Function | biotin carboxylase activity | |
Molecular Function | metal ion binding | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | malonyl-CoA biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBiotin carboxylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionQ8X9B6
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000146792 | 1-449 | Biotin carboxylase | |||
Sequence: MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNSIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQEK |
Interaction
Subunit
Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-445 | Biotin carboxylation | ||||
Sequence: MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNSIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLG | ||||||
Domain | 120-317 | ATP-grasp | ||||
Sequence: IAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNSIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAA |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)49,337
- Last updated2002-03-05 v1
- ChecksumBC5716323F6233ED
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE005174 EMBL· GenBank· DDBJ | AAG58384.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BA000007 EMBL· GenBank· DDBJ | BAB37551.1 EMBL· GenBank· DDBJ | Genomic DNA |