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Q8FXY7 (ACCD_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceInferred 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 HAMAP-Rule MF_01395.

Sequence similarities

Belongs to the AccD/PCCB family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

malonyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentacetyl-CoA carboxylase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 301301Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395
PRO_0000389707

Sequences

Sequence LengthMass (Da)Tools
Q8FXY7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: BCB69B33AEA8D566

FASTA30133,270
        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 

« Hide

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. expand/collapse author list , 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.
PIRAF3504.
RefSeqNP_699082.1. NC_004310.3.
YP_005616906.1. NC_017251.1.

3D structure databases

ProteinModelPortalQ8FXY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR2107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN30997; AAN30997; BR2107.
AEM19414; AEM19414; BS1330_I2101.
GeneID1167810.
12137890.
KEGGbms:BR2107.
bsi:BS1330_I2101.
PATRIC17792647. VBIBruSui107850_2144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0777.
HOGENOMHOG000021670.
KOK01963.
OMAGLWIKCP.
OrthoDBEOG6HQSSF.
ProtClustDBPRK05654.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Family and domain databases

HAMAPMF_01395. AcetylCoA_CT_beta.
InterProIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR011762. COA_CT_N.
[Graphical view]
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSPR01070. ACCCTRFRASEB.
TIGRFAMsTIGR00515. accD. 1 hit.
PROSITEPS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCD_BRUSU
AccessionPrimary (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: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella suis

Brucella suis (strain 1330): entries and gene names