A9HE81 (ACCD_GLUDA) 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:	GDI1253, Gdia_1964

Organism

Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]

Taxonomic identifier

272568 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter › Gluconacetobacter diazotrophicus

Protein attributes

Sequence length	300 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.
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.
Sequence similarities	Belongs to the AccD/PCCB family.
Sequence caution	The sequence CAP55196.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 300	300	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395		PRO_0000389749
Regions
	Zinc finger	28 – 50	23	C4-type By similarity
Sites
	Metal binding	28	1	Zinc By similarity
	Metal binding	31	1	Zinc By similarity
	Metal binding	47	1	Zinc By similarity
	Metal binding	50	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9HE81 [UniParc]. Last modified December 15, 2009. Version 2. Checksum: B7BFBB024ACBDFEB	FASTA	300	32,820
	10 20 30 40 50 60 MSWLTEYVRP KIRGLLKREV PDNLWTNCES CSQMILVKDL QKAMNVCPHC GHHMRASVAE 70 80 90 100 110 120 RFGWTFDEGT FTRIELPKVP VDPLSFRDRK RYTERLKDER SKSQLDESMA VAHGRIGGHD 130 140 150 160 170 180 AVVAVMAFEF IAGTMGAALG EAFLAAARLA ILQKAPLVVF TASGGARMQE GMVSLMQMPR 190 200 210 220 230 240 TTVAVQMLRD AGLPYIVVLT NPTTGGVTAS FAMLGDVQIS EPNALIGFAG QRVIEDTVRE 250 260 270 280 290 300 KLPEGFQRAE YLLDHGMIDM VVKRPALPEM LGRLIGLMNH RHVNAPGAAL GGAAPVRPAA

References

[1]

"Gluconacetobacter diazotrophicus Pal5 complete genome." Bertalan M., Baldani I.J., Ferreira P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49037 / DSM 5601 / PAl5.

[2]

"Complete sequence of chromosome of Gluconacetobacter diazotrophicus PAl 5." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Triplett E.W. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49037 / DSM 5601 / PAl5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM889285 Genomic DNA. Translation: CAP55196.1. Different initiation. CP001189 Genomic DNA. Translation: ACI51724.1.
RefSeq	YP_001601509.1. NC_010125.1. YP_002276339.1. NC_011365.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	272568.GDI_1253.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACI51724; ACI51724; Gdia_1964. CAP55196; CAP55196; GDI1253.
GeneID	5789173. 6975390.
KEGG	gdi:GDI_1253. gdj:Gdia_1964.
PATRIC	22052348. VBIGluDia203729_1957.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0777.
HOGENOM	HOG000021670.
KO	K01963.
ProtClustDB	CLSK936299.
Enzyme and pathway databases
BioCyc	GDIA272568:GJPS-1275-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_GLUDA

Accession

Primary (citable) accession number: A9HE81
Secondary accession number(s): B5ZCR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	December 15, 2009
Last modified:	May 1, 2013
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program