Reviewed, UniProtKB/Swiss-Prot O52058 (ACCC_CHRVI)

Names and origin

Protein names

Recommended name:
    Biotin carboxylase
    EC=6.3.4.14
Alternative name(s):
    Acetyl-CoA carboxylase subunit A
      Short name=ACC
    EC=6.4.1.2

Gene names

Name:

accC

Organism

Chromatium vinosum (Allochromatium vinosum)

Taxonomic identifier

1049 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium

Protein attributes

Sequence length	140 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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 By similarity.
Catalytic activity	ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	Acetyl-CoA carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex By similarity.
Sequence similarities	Contains 1 biotin carboxylation domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC biotin binding Inferred from electronic annotation. Source: InterPro biotin carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 140	›140	Biotin carboxylase		PRO_0000146790
Regions
	Domain	‹1 – 139	›139	Biotin carboxylation
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	O52058-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F2C4ECB95D87D505	FASTA	140	15,595
	10 20 30 40 50 60 VDIVKEQILI AAGEPLRYRQ SDIQMRGHAI ECRINAEHPE TFMPSPGKIT DFHAPGGPGV 70 80 90 100 110 120 RIETHIYSGY TVPCHYDSMI GKLITHGEDR ESAVARMCNA LRETVIEGIH SNIKLQRSLM 130 140 RDGAFLAGAN IHYLEKMLGL

References

[1]

"Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum." Pattaragulwanit K., Brune D.C., Trueper H.G., Dahl C. Arch. Microbiol. 169:434-444(1998) [PubMed: 9560425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / D.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF017119 Genomic DNA. Translation: AAB91545.1.
3D structure databases
HSSP	HSSP built from PDB template 1DV1 based on UniProtKB P24182.
SMR	O52058. Positions 1-140.
ModBase	Search...
Enzyme and pathway databases
BRENDA	6.3.4.14. 2799. 6.4.1.2. 2799.
Family and domain databases
InterPro	IPR013816. ATP_grasp_subdomain_2. IPR011764. BC. IPR005482. Biotin_COase_C. IPR005479. CarbamoylP_synth_lsu_ATP-bd. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
Pfam	PF02785. Biotin_carb_C. 1 hit. [Graphical view]
PROSITE	PS50979. BC. 1 hit. PS00866. CPSASE_1. Partial match. PS00867. CPSASE_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCC_CHRVI

Accession

Primary (citable) accession number: O52058

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)