Reviewed, UniProtKB/Swiss-Prot Q8U9U5 (ACCA_AGRT5)

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:	Atu3630
ORF Names:	AGR_L_2394

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	317 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 – 317	317	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_0000223724

Sequences

	Sequence		Length	Mass (Da)
	Q8U9U5-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: F226EF4717846846	FASTA	317	34,542
	10 20 30 40 50 60 MHNYLDFEKP ISDLEGKIIE LKKLADEDES IDTSEEINRL ESRVNDAMQD IYSKLNAWQK 70 80 90 100 110 120 TQVARHPQRP HFVDYAKSLF TDFTPLAGDR KFSEDAAIQA GLARFNGQPV AIIGQEKGND 130 140 150 160 170 180 TKSRLKHNFG SARPEGYRKA IRVLELADRF SLPVVTLIDT AGAYPGVGAE ERGQAEAIAR 190 200 210 220 230 240 STEMCLNVKV PIVSVVIGEG GSGGAIAIAT GNRVYMLEHS VYSVISPEGA ASILWRDSTR 250 260 270 280 290 300 AKEAATNMKI TSEDLKSLGV IDGIIPEPIG GAHRAPETVI SATGDVIAKA LADLSQRSGT 310 QLRAERRQKF LDIGRNL

References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE007870 Genomic DNA. Translation: AAK89767.1.
PIR	AD3003. E98280.
RefSeq	NP_356982.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1135504.
GenomeReviews	Gene locus Atu3630 in contig AE007870_GR.
KEGG	atc:AGR_L_2394. atu:Atu3630.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8U9U5.
OMA	Q8U9U5. 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_AGRT5

Accession

Primary (citable) accession number: Q8U9U5
Secondary accession number(s): Q7CSY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 39 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)