Q8FXY7 (ACCD_BRUSU) 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:	BR2107, BS1330_I2101

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	301 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
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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
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 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395		PRO_0000389707

Sequences

	Sequence		Length	Mass (Da)
	Q8FXY7 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: BCB69B33AEA8D566	FASTA	301	33,270
	10 20 30 40 50 60 MNWITNYVRP KINSMLGRRE MPENLWIKDP STGEMVFHKD LESNQFVIPS SGHHMRIKAK 70 80 90 100 110 120 DRLRFFFDNG EYTTLEAPKV PLDPLKFRDE KKYIDRLKDY RSRTGMDDAI VNGLGTIEGL 130 140 150 160 170 180 PIVATVQDFS FMGGSLGMGA GEAIIQGFEK AIELKRPLVL FASSGGARMQ EGILSLMQLP 190 200 210 220 230 240 RTTVAVEMLK EAGLPYIVVL TNPTTGGVTA SYAMLGDIHI AEPGALIGFA GPRVIEQTIR 250 260 270 280 290 300 EKLPEGFQSS EYLMEHGMVD MVVSRLELKA TIARLLKIMT KQPANSDAPA PQKPDADSKA A

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN30997.1. CP002997 Genomic DNA. Translation: AEM19414.1.
PIR	AF3504.
RefSeq	NP_699082.1. NC_004310.3. YP_005616906.1. NC_017251.1.
3D structure databases
ProteinModelPortal	Q8FXY7.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR2107.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN30997; AAN30997; BR2107. AEM19414; AEM19414; BS1330_I2101.
GeneID	1167810. 12137890.
KEGG	bms:BR2107. bsi:BS1330_I2101.
PATRIC	17792647. VBIBruSui107850_2144.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0777.
HOGENOM	HOG000021670.
KO	K01963.
OMA	GLWIKCP.
ProtClustDB	PRK05654.
Enzyme and pathway databases
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_BRUSU

Accession

Primary (citable) accession number: Q8FXY7
Secondary accession number(s): G0K955

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program