P37798 · ACCC_PSEAE
- ProteinBiotin carboxylase
- GeneaccC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids449 (go to sequence)
- Protein existenceEvidence at protein level
- 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: EKFL | ||||||
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP37798
Proteomes
Organism-specific databases
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000146794 | 1-449 | Biotin carboxylase | |||
Sequence: MLEKVLIANRGEIALRILRACKELGIKTVAVHSTADRELMHLSLADESVCIGPAPATQSYLQIPAIIAAAEVTGATAIHPGYGFLAENADFAEQIERSGFTFVGPTAEVIRLMGDKVSAKDAMKRAGVPTVPGSDGPLPEDEETALAIAREVGYPVIIKAAGGGGGRGMRVVYDESELIKSAKLTRTEAGAAFGNPMVYLEKFLTNPRHVEVQVLSDGQGNAIHLGDRDCSLQRRHQKVIEEAPAPGIDEKARQEVFARCVQACIEIGYRGAGTFEFLYENGRFYFIEMNTRVQVEHPVSEMVTGVDIVKEMLRIASGEKLSIRQEDVVIRGHALECRINAEDPKTFMPSPGKVKHFHAPGGNGVRVDSHLYSGYSVPPNYDSLVGKVITYGADRDEALARMRNALDELIVDGIKTNTELHKDLVRDAAFCKGGVNIHYLEKKLGMDKH |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-445 | Biotin carboxylation | ||||
Sequence: MLEKVLIANRGEIALRILRACKELGIKTVAVHSTADRELMHLSLADESVCIGPAPATQSYLQIPAIIAAAEVTGATAIHPGYGFLAENADFAEQIERSGFTFVGPTAEVIRLMGDKVSAKDAMKRAGVPTVPGSDGPLPEDEETALAIAREVGYPVIIKAAGGGGGRGMRVVYDESELIKSAKLTRTEAGAAFGNPMVYLEKFLTNPRHVEVQVLSDGQGNAIHLGDRDCSLQRRHQKVIEEAPAPGIDEKARQEVFARCVQACIEIGYRGAGTFEFLYENGRFYFIEMNTRVQVEHPVSEMVTGVDIVKEMLRIASGEKLSIRQEDVVIRGHALECRINAEDPKTFMPSPGKVKHFHAPGGNGVRVDSHLYSGYSVPPNYDSLVGKVITYGADRDEALARMRNALDELIVDGIKTNTELHKDLVRDAAFCKGGVNIHYLEKKLG | ||||||
Domain | 120-317 | ATP-grasp | ||||
Sequence: KDAMKRAGVPTVPGSDGPLPEDEETALAIAREVGYPVIIKAAGGGGGRGMRVVYDESELIKSAKLTRTEAGAAFGNPMVYLEKFLTNPRHVEVQVLSDGQGNAIHLGDRDCSLQRRHQKVIEEAPAPGIDEKARQEVFARCVQACIEIGYRGAGTFEFLYENGRFYFIEMNTRVQVEHPVSEMVTGVDIVKEMLRIAS |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)48,888
- Last updated1994-10-01 v1
- Checksum3B04C77785C73541
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L14612 EMBL· GenBank· DDBJ | AAA16041.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG08233.1 EMBL· GenBank· DDBJ | Genomic DNA |