Reviewed, UniProtKB/Swiss-Prot B0CJD4 (ACCA_BRUSI)

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:	BSUIS_A1873

Organism

Brucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP]

Taxonomic identifier

470137 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	317 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 – 317	317	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_1000083921

Sequences

	Sequence		Length	Mass (Da)
	B0CJD4-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 28D0B15DD22C6786	FASTA	317	35,013
	10 20 30 40 50 60 MYNYLDFEKP VADLEGQILE LKKLAQEQGS VEMGDEISRL EKRSADALKD IYRKLTPWQK 70 80 90 100 110 120 AQIARHPDRP HCLEYIDRLF TEFTPLAGDR KFANDEALQA GFGRFNGTPV AIIGQEKGSD 130 140 150 160 170 180 TKTRLKHNFG SARPEGYRKA VRIMEMADRF QLPLITFVDT AGAYPGVSAE ERGQAEAIAR 190 200 210 220 230 240 STAECLKLRV PVISIIIGEG GSGGAIAIAV ANRVYMLEHS IYSVISPEGA ASILWHDSTR 250 260 270 280 290 300 AKDAASNMRI TAQDLFDLKI IDGIIPEPLG GAHRGKESVI DATGDIIAAS LRSMKDIDGE 310 TLKQERRQKF LEIGRNI

References

[1]

"Brucella suis ATCC 23445 whole genome shotgun sequencing project." Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000911 Genomic DNA. Translation: ABY38886.1.
RefSeq	YP_001628456.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5837377.
GenomeReviews	Gene locus BSUIS_A1873 in contig CP000911_GR.
KEGG	bmt:BSUIS_A1873.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	B0CJD4. HSVYTVA.
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_BRUSI

Accession

Primary (citable) accession number: B0CJD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 12 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)