Reviewed, UniProtKB/Swiss-Prot Q0VQE1 (ACCA_ALCBS)

Names and origin

Protein names

Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
      Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha
      Short name=ACCase subunit alpha
    EC=6.4.1.2

Gene names

Name:	accA
Ordered Locus Names:	ABO_1159

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA By similarity.
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_00823
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823
Subunit structure	Acetyl-CoA carboxylase is an heterohexamer composed of biotin carboxyl carrier protein (accB), biotin carboxylase (accC) and two subunits each of ACCase subunit alpha (accA) and ACCase subunit beta (accD) By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the accA family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_1000062572

Sequences

	Sequence		Length	Mass (Da)
	Q0VQE1-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 5AE1E996405EBDFD	FASTA	323	35,719
	10 20 30 40 50 60 MNPNFLEFEQ PIADLEAKIE ELRLVGSGSD INISEEVAKL QEKSITLTES IFRGLSSWQI 70 80 90 100 110 120 SQLSRHPKRP YMLDYIKRIF TDFDELHGDR AFSDDPAIIG GMTRLNGQPV MVIGHQKGRE 130 140 150 160 170 180 VKEKVRRNFG MPKPEGYRKA LRLMEMAERF KLPVLTFIDT PGAFPGIDAE ERGQSEAIAR 190 200 210 220 230 240 NLRVMSQLKT PILATVIGEG GSGGALAIGV CDHLQMLEFS TYSVISPEGC ASILWRSADK 250 260 270 280 290 300 APEAAQAMGL TAGRLHELGI VDQVIKEPLG GAHRDYDQAA DAIRKALAAQ LESLCSMETD 310 320 ALINRRYERL MSYGNVVSDP ADE

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL16607.1.
RefSeq	YP_692879.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4211797.
GenomeReviews	Gene locus ABO_1159 in contig AM286690_GR.
KEGG	abo:ABO_1159.
NMPDR	fig|393595.12.peg.1170.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VQE1.
OMA	Q0VQE1. HSVYTVA.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1159-MON.
Family and domain databases
HAMAP	MF_00823. [Tree]
InterPro	IPR001095. Acetyl_CoA_COase_a_su. IPR011763. COA_CT_C. [Graphical view]
PANTHER	PTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
Pfam	PF03255. ACCA. 1 hit. [Graphical view]
PRINTS	PR01069. ACCCTRFRASEA.
TIGRFAMs	TIGR00513. accA. 1 hit.
PROSITE	PS50989. COA_CT_CTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCA_ALCBS

Accession

Primary (citable) accession number: Q0VQE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 23 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)