Reviewed, UniProtKB/Swiss-Prot A5G0K5 (ACCA_ACICJ)

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:	Acry_2189

Organism

Acidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]

Taxonomic identifier

349163 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

Protein attributes

Sequence length	318 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 – 318	318	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_1000072877

Sequences

	Sequence		Length	Mass (Da)
	A5G0K5-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 3F718433096BD6F3	FASTA	318	34,106
	10 20 30 40 50 60 MRHFLDFEKP VAELEAKIEE LRRMTDPGEL NIAEEVTLLS DKAERQLRTL YGRLSPWQKT 70 80 90 100 110 120 QVARHPERPK ARDVIAGLIT EFTPLAGDRG FGEDAAIVAG PGRFKGEPVM VIAIEKGWDL 130 140 150 160 170 180 ESRLKHNFGS PRPEGYRKAR RLIEMAGRFG LPVLSFVDTS GAYPGVDAEA RGQAEAIARG 190 200 210 220 230 240 IDACLAAPVP FIATIIGEGG SGGAIAIAAA DTVLMFEHAI YSVISPEGCA AILWEDRANA 250 260 270 280 290 300 AQAAEAMKIT AQDLKRLGII DRIVPEPLGG AHRDPQAAIT ALGAAIAETL PGLAALAPEA 310 LRAKRREKFL AIGQTLPV

References

[1]

"Complete sequence of chromosome of Acidiphilium cryptum JF-5." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000697 Genomic DNA. Translation: ABQ31387.1.
RefSeq	YP_001235306.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5G0K5.
Genome annotation databases
GeneID	5162553.
GenomeReviews	Gene locus Acry_2189 in contig CP000697_GR.
KEGG	acr:Acry_2189.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	HSVYTVA.
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. IPR001753. Crotonase_core. [Graphical view]
PANTHER	PTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
Pfam	PF03255. ACCA. 1 hit. PF00378. ECH. 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_ACICJ

Accession

Primary (citable) accession number: A5G0K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 18 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)