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Reviewed, UniProtKB/Swiss-Prot B2S8T2 (ACCA_BRUA1)

Last modified November 3, 2009. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: BAbS19_I19040
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP]
Taxonomic identifier430066 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000134461

Sequences

Sequence LengthMass (Da)Tools
B2S8T2-1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 28D0ACEB095C6786

FASTA31734,983
        10         20         30         40         50         60 
MYNYLDFEKP VADLEGQILE LKKLAQEQGS VEMGDEISRL EKRSADALKD IYRKLTPWQK 

        70         80         90        100        110        120 
AQIARHPDRP HCLEYIDRLF TEFTPLAGDR KFANDEALQA GFGRFNGTPV AIIGQEKGSD 

       130        140        150        160        170        180 
TKTRLKHNFG SARPEGYRKA VRIMEMADRF QLPLITFVDT AGAYPGVSAE ERGQAEAIAR 

       190        200        210        220        230        240 
STAECLKLRV PVISIIIGEG GSGGAIAIAV ANRVYMLEHS IYSVISPEGA ASILWHDSTR 

       250        260        270        280        290        300 
AKDAASNMRI TAQDLFDLKI IDGIIPEPLG GAHRGKESVI DAAGDIIAAS LRSMKDIDGE 

       310 
TLKQERRQKF LEIGRNI 

« Hide

References

[1]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed: 18478107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000887 Genomic DNA. Translation: ACD73386.1.
RefSeqYP_001935860.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6327006.
GenomeReviewsGene locus BAbS19_I19040 in contig CP000887_GR.
KEGGbmc:BAbS19_I19040.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAHSVYTVA.

Family and domain databases

HAMAPMF_00823.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR020582. Acetyl_CoA_COase_a_su_cons-reg.
IPR011763. COA_CT_C.
[Graphical view]
PANTHERPTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
PfamPF03255. ACCA. 1 hit.
[Graphical view]
PRINTSPR01069. ACCCTRFRASEA.
TIGRFAMsTIGR00513. accA. 1 hit.
PROSITEPS50989. COA_CT_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCA_BRUA1
AccessionPrimary (citable) accession number: B2S8T2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: November 3, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents