Reviewed, UniProtKB/Swiss-Prot Q63ST0 (ACCA_BURPS)

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:	BPSL2241

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	323 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. HAMAP MF_00823
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: 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_0000223746

Sequences

	Sequence		Length	Mass (Da)
	Q63ST0-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 2A95695D449EF04F	FASTA	323	35,667
	10 20 30 40 50 60 MKTTFLDFEQ PIAELEAKIE ELRFVQDDSA VDISEEIERL SKKSQQLTKD LYANLTPWQV 70 80 90 100 110 120 SQIARHPQRP YTLDYVSELF TDFHELHGDR AFADDQSIVG GLARFNGHAC MVIGHQKGRD 130 140 150 160 170 180 TKERAARNFG MPRPEGYRKA ERLMRVAEKF GLPIFTFVDT PGAYPGVGAE ERGQSEAIGH 190 200 210 220 230 240 NLYVMAELKT PIIATVIGEG GSGGALAIAV ADTVMMLQFS TYSVISPEGC ASILWKSAAK 250 260 270 280 290 300 APEAAEALGL TAHRLKALGL IDKIVNEPLG GAHRDPKGMA ALLRRALGDS LRQFQGMSVD 310 320 ALRERRFERL MAYGKFKETT PRA

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH36243.1.
RefSeq	YP_108836.1.
3D structure databases
SMR	Q63ST0. Positions 5-314.
ModBase	Search...
Genome annotation databases
GeneID	3092968.
GenomeReviews	Gene locus BPSL2241 in contig BX571965_GR.
KEGG	bps:BPSL2241.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG286557.
OMA	HSVYTVA.
PhylomeDB	Q63ST0.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL2241-MONOMER.
BRENDA	6.4.1.2. 275934.
Family and domain databases
HAMAP	MF_00823. AcetylCoA_CT_alpha. [Tree]
InterPro	IPR001095. Acetyl_CoA_COase_a_su. IPR020582. Acetyl_CoA_COase_a_su_cons-reg. 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_BURPS

Accession

Primary (citable) accession number: Q63ST0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	October 25, 2004
Last modified:	February 9, 2010
This is version 35 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)