A2CAG3 (ACCD_PROM3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Short name=ACCase subunit beta
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit beta
EC=6.4.1.2

Gene names

Name:	accD
Ordered Locus Names:	P9303_17311

Organism

Prochlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]

Taxonomic identifier

59922 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus › Prochlorococcus marinus

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP-Rule MF_01395
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP-Rule MF_01395
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01395
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP-Rule MF_01395
Subunit structure	Acetyl-CoA carboxylase is a 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 HAMAP-Rule MF_01395.
Sequence similarities	Belongs to the AccD/PCCB family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 zinc ion binding 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 – 293	293	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395		PRO_0000359022
Regions
	Zinc finger	33 – 55	23	C4-type Potential
Sites
	Metal binding	33	1	Zinc By similarity
	Metal binding	36	1	Zinc By similarity
	Metal binding	52	1	Zinc By similarity
	Metal binding	55	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2CAG3 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 4E5D5FAEC4EDFA81	FASTA	293	32,212
	10 20 30 40 50 60 MSLFDWFADR RKGQFVGKVS QETEESDGLW VKCPECGQVV YRKDLHANAS VCSNCGYHHR 70 80 90 100 110 120 IDSDERIVLI ADQGSFKSLD RNLSPTDPLG FKDRRAYADR LRESQASTGM KDGVVTGLCQ 130 140 150 160 170 180 VEGMPMAMAV MDFRFMGGSM GSVVGEKITR LVERATAQGL PLLIVCASGG ARMQEGMLSL 190 200 210 220 230 240 MQMAKISGAL ERHREAELLY MPLLTHPTTG GVTASFAMLG DLILAEPKAL IGFAGRRVIE 250 260 270 280 290 QTLREKLPDN FQTAEYLQEH GFVDTIVPRT QLRKTLASLL LLHGCKAKKA AGK

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000554 Genomic DNA. Translation: ABM78473.1.
RefSeq	YP_001017738.1. NC_008820.1.
3D structure databases
ProteinModelPortal	A2CAG3.
SMR	A2CAG3. Positions 26-284.
ModBase	Search...
Protein-protein interaction databases
STRING	59922.P9303_17311.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM78473; ABM78473; P9303_17311.
GeneID	4776173.
KEGG	pmf:P9303_17311.
PATRIC	23000944. VBIProMar17757_1782.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0777.
HOGENOM	HOG000021671.
KO	K01963.
OMA	GLWIKCP.
ProtClustDB	PRK05654.
Enzyme and pathway databases
BioCyc	PMAR59922:GH54-1825-MONOMER.
UniPathway	UPA00655; UER00711.
Family and domain databases
HAMAP	MF_01395. AcetylCoA_CT_beta.
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011762. COA_CT_N. [Graphical view]
Pfam	PF01039. Carboxyl_trans. 1 hit. [Graphical view]
PRINTS	PR01070. ACCCTRFRASEB.
TIGRFAMs	TIGR00515. accD. 1 hit.
PROSITE	PS50980. COA_CT_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCD_PROM3

Accession

Primary (citable) accession number: A2CAG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program