Reviewed, UniProtKB/Swiss-Prot Q1LSU5 (ACCA_BAUCH)

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:	BCI_0539

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	319 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 – 319	319	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_1000062580

Sequences

	Sequence		Length	Mass (Da)
	Q1LSU5-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 26D2CA22AD8E548B	FASTA	319	35,638
	10 20 30 40 50 60 MSINFIDFEQ PIADIEAKIE SLTSISSIDK TCDTNFNEEI KRLRDKSIEL TRKIFAHLSA 70 80 90 100 110 120 WQIAQLARHP CRPYMLDYVQ YIFTDFDELA GDRAYADDKA IVGGLARINS RPVMIIGHQK 130 140 150 160 170 180 GREIKEKIRR NFGMPAPEGY RKALRLMKMA DRFSIPILTF IDTPGAYPGI GAEERGQSEA 190 200 210 220 230 240 IATNLREMAY LRVPIVSTII GEGGSGGALA IGVGDKVNML KYSTYSVISP EGCASILWKS 250 260 270 280 290 300 VDKAPLAAEA MGINAARLKK LKLIDSIIPE PLGGAHRDVA IMAASLKKQL LFDLSELDRM 310 NEQELLDRRY NRIMKYGYC

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF13894.1.
RefSeq	YP_588969.1.
3D structure databases
SMR	Q1LSU5. Positions 4-318.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LSU5.
Genome annotation databases
GeneID	4056479.
GenomeReviews	Gene locus BCI_0539 in contig CP000238_GR.
KEGG	bci:BCI_0539.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0825.
HOGENOM	HBG286557.
OMA	HSVYTVA.
PhylomeDB	Q1LSU5.
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_BAUCH

Accession

Primary (citable) accession number: Q1LSU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 30, 2006
Last modified:	February 9, 2010
This is version 29 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)