Q8FY57 (ACCA_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	accA
Ordered Locus Names:	BR2032, BS1330_I2026

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
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. HAMAP MF_00823
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 HAMAP MF_00823.
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: UniProtKB-KW
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: EC
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_0000223744

Sequences

	Sequence		Length	Mass (Da)
	Q8FY57 [UniParc]. Last modified March 1, 2003. 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]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN30922.1. CP002997 Genomic DNA. Translation: AEM19339.1.
PIR	AB3257.
RefSeq	NP_699007.1. NC_004310.3.
3D structure databases
ProteinModelPortal	Q8FY57.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1167734.
GenomeReviews	Gene locus BR2032 in contig AE014291_GR.
KEGG	bms:BR2032.
PATRIC	17792491. VBIBruSui107850_2067.
TIGR	BR2032.
Phylogenomic databases
HOGENOM	HBG286557.
OMA	GRDTKDN.
PhylomeDB	Q8FY57.
ProtClustDB	PRK05724.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_2032-MONOMER.
Family and domain databases
HAMAP	MF_00823. AcetylCoA_CT_alpha. [Tree]
InterPro	IPR001095. Acetyl_CoA_COase_a_su. IPR011763. COA_CT_C. [Graphical view]
KO	K01962.
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_BRUSU

Accession

Primary (citable) accession number: Q8FY57
Secondary accession number(s): G0K8Q2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program