Reviewed, UniProtKB/Swiss-Prot O34847 (ACCA_BACSU)

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:	BSU29200

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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
Enzyme regulation	Inhibited by pyrrolidine dione antibiotics moiramide B (CPD1) and CPD2. Ref.3
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	Antibiotic resistance 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 response to antibiotic 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 325	325	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_0000146773
Experimental info
	Mutagenesis	199	1	G → S: Resistant to the pyrrolidine dione antibiotic CPD2. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O34847-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 9B177DEE4A5B5864	FASTA	325	36,334
	10 20 30 40 50 60 MAPRLEFEKP VIELQTKIAE LKKFTQDSDM DLSAEIERLE DRLAKLQDDI YKNLKPWDRV 70 80 90 100 110 120 QIARLADRPT TLDYIEHLFT DFFECHGDRA YGDDEAIVGG IAKFHGLPVT VIGHQRGKDT 130 140 150 160 170 180 KENLVRNFGM PHPEGYRKAL RLMKQADKFN RPIICFIDTK GAYPGRAAEE RGQSEAIAKN 190 200 210 220 230 240 LFEMAGLRVP VICIVIGEGG SGGALGLGVG NHLHMLENST YSVISPEGAA ALLWKDSSLA 250 260 270 280 290 300 KKAAETMKIT APDLKELGII DHMIKEVKGG AHHDVKLQAS YMDETLKQSL KTLLKLSEEE 310 320 LVQQRYEKYK AIGKVSVEDQ YIGVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity." Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M., Raabe M., Haebich D., Ziegelbauer K. J. Biol. Chem. 279:26066-26073(2004) [PubMed: 15066985] [Abstract] Cited for: ENZYME REGULATION, ANTIBIOTIC RESISTANCE, MUTAGENESIS OF GLY-199.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF008220 Genomic DNA. Translation: AAC00341.1. AL009126 Genomic DNA. Translation: CAB14880.1.
PIR	G69580.
RefSeq	NP_390798.1.
3D structure databases
SMR	O34847. Positions 1-313.
ModBase	Search...
Genome annotation databases
GeneID	936367.
GenomeReviews	Gene locus BSU29200 in contig AL009126_GR.
KEGG	bsu:BSU29200.
NMPDR	fig|224308.1.peg.2923.
Organism-specific databases
SubtiList	BG12557. accA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	HBG286557.
OMA	HSVYTVA.
PhylomeDB	O34847.
Enzyme and pathway databases
BRENDA	6.4.1.2. 150.
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_BACSU

Accession

Primary (citable) accession number: O34847

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 73 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)