Reviewed, UniProtKB/Swiss-Prot Q633J7 (ACCA_BACCZ)

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:	BCE33L4341

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	324 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 – 324	324	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_0000223731

Sequences

	Sequence		Length	Mass (Da)
	Q633J7-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 25A45F26634206E3	FASTA	324	36,470
	10 20 30 40 50 60 MAELEFEKPV VELRNKIREL KDYTKNSQMD FSEEIRILED KLENLEEDIY GNMKVWDRVQ 70 80 90 100 110 120 IARHAERPTT LDYIEHLFTD FFECHGDRLF GDDAAIVGGI AKYKGMPVTV IGHQRGKDTK 130 140 150 160 170 180 ENIRRNFGMP HPEGYRKALR LMKQAEKFNR PIICFIDTKG AYPGKAAEER GQSEAIARNL 190 200 210 220 230 240 FEMAGLTVPV ICIVIGEGGS GGALGLGVGD YIHMLENSTY SVITPEGAAA ILWKDAGKAK 250 260 270 280 290 300 EAAEAMRITA ADLKELGVID EIIPEAKGGA HRNVLKQSEN IDLMLRKTFE QLNGISKDEL 310 320 IEKRYEKYMK IGQVSFSNAS IWIK

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000001 Genomic DNA. Translation: AAU15929.1.
RefSeq	YP_085920.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q633J7.
Genome annotation databases
GeneID	3026819.
GenomeReviews	Gene locus BCE33L4341 in contig CP000001_GR.
KEGG	bcz:BCZK4341.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q633J7.
OMA	HSVYTVA.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L4341-MON.
Family and domain databases
HAMAP	MF_00823. [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_BACCZ

Accession

Primary (citable) accession number: Q633J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 33 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)