Reviewed, UniProtKB/Swiss-Prot Q2KX40 (ACCA_BORA1)

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:	BAV2560

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	321 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 – 321	321	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_1000062581

Sequences

	Sequence		Length	Mass (Da)
	Q2KX40-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: D6411309F209069A	FASTA	321	35,845
	10 20 30 40 50 60 MRNTFLEFEQ PLAELENKIE QLRYVQADSA VDISDEIGRL QQKSQTLAKE IYGKLTPWQT 70 80 90 100 110 120 ALVARHPQRP YTLDYVREIF TDFHELHGDR MYADDQSIVG GLARFNGQSC MVIGHQKGRD 130 140 150 160 170 180 TKERAARNFG MPRPEGYRKA QRLMRLAEKF KLPIFTFVDT PGAYPGIGAE ERGQSEAIGH 190 200 210 220 230 240 NLYVMAELKV PVIVTIIGEG GSGGALAIAV GNAVLMLQYS TYSVISPEGC ASILWRSADK 250 260 270 280 290 300 APEAAEALAI TAPRLKDLGL IDRVVNEPIG GAHRDPRVMA RLLRRALGDS LRQLQDLTPE 310 320 QLVEQRLERV LAYGRFQEVR G

References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM167904 Genomic DNA. Translation: CAJ50170.1.
RefSeq	YP_787068.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6267333.
GenomeReviews	Gene locus BAV2560 in contig AM167904_GR.
KEGG	bav:BAV2560.
NMPDR	fig|521.1.peg.242.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2KX40.
OMA	Q2KX40. 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_BORA1

Accession

Primary (citable) accession number: Q2KX40

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	March 7, 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)