Q9KDS9 (ACCC_BACHD) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	BH1132

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
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 + carboxy-biotin-[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 ATP-grasp domain. Contains 1 biotin carboxylation domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
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 carboxylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Biotin carboxylase		PRO_0000146788
Regions
	Domain	1 – 445	445	Biotin carboxylation
	Domain	120 – 317	198	ATP-grasp
Sites
	Active site	292	1	By similarity
	Binding site	116	1	ATP By similarity
	Binding site	200	1	ATP By similarity
	Binding site	235	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KDS9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4BCF230D1A44E880	FASTA	452	49,938
	10 20 30 40 50 60 MFKKVLIANR GEIAVRIIRT CQKLNIRTVA IYSEADVDSL HVKHADEAFL IGKPPVAESY 70 80 90 100 110 120 LKVDTILEVA KQAGVDAIHP GYGLLSENAR FARACVEAGI SFIGPSPEVI ERMGSKIAAR 130 140 150 160 170 180 TAMQTAGVPV IPGSDVALAD EEEAVHLARK FGYPVMLKAS AGGGGIGMQL VRNDEEMRKA 190 200 210 220 230 240 FAGNQKRATS FFGDGTMFLE KAVENPRHIE VQIAADHHGH VVHLWERDCS IQRRHQKVVE 250 260 270 280 290 300 EAPSPFVDEA LREKIGQLAV KAAKAIDYRN LGTVECLVDG EKNIYFLEMN TRLQVEHPVT 310 320 330 340 350 360 EEITGIDLVE WQLLIAAGEQ LPYAQHEIPL QGHAIEVRIY AEDPVTFFPS PGMIKRFTLP 370 380 390 400 410 420 EGEGIRHEYA ISEGYKVTPF YDPMVAKLIV SADTRGEAIQ RLGRALKQYE IEGIKTNIPM 430 440 450 LKQVINHPVF QAGEATTAFV TNHLKVKTGR NP

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB04851.1.
PIR	D83791.
RefSeq	NP_241998.1. NC_002570.2.
3D structure databases
ProteinModelPortal	Q9KDS9.
SMR	Q9KDS9. Positions 1-444.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000053957; EBBACP00000052596; EBBACG00000053948.
GeneID	894101.
GenomeReviews	Gene locus BH1132 in contig BA000004_GR.
KEGG	bha:BH1132.
NMPDR	fig|272558.1.peg.1132.
PATRIC	18939326. VBIBacHal18977_1181.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001329.
HOGENOM	HBG535236.
OMA	MQLVRND.
PhylomeDB	Q9KDS9.
ProtClustDB	PRK06111.
Enzyme and pathway databases
BioCyc	BHAL272558:BH1132-MONOMER.
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KO	K01961.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCC_BACHD

Accession

Primary (citable) accession number: Q9KDS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program