Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B2JIR9 (ACCA_BURP8)

Last modified November 3, 2009. Version 12. 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: Bphy_1388
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length323 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 – 323323Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000134466

Sequences

Sequence LengthMass (Da)Tools
B2JIR9-1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 42DDA8204A01F045

FASTA32335,789
        10         20         30         40         50         60 
MKTTFLDFEQ PIAELEAKIE ELRFVQDDSA VDISEEIERL SKKSQQLTKD LYTNLTPWQV 

        70         80         90        100        110        120 
SQIARHPQRP YTQDYINELF TDFHELHGDR SFADDLSIVG GLARFNGQPC MVIGHQKGRD 

       130        140        150        160        170        180 
TKERALRNFG MPRPEGYRKA ERLMRLAEKF GLPLFTFIDT PGAYPGIGAE ERGQSEAIGR 

       190        200        210        220        230        240 
NLYVMAELKT PIISTVIGEG GSGGALAVAV ADSVLMLQFS TYSVISPEGC ASILWKSAAK 

       250        260        270        280        290        300 
APEAAEALGL TAHRLKALGL IDKIVSEPLG GAHRDPKGMA AMLRRALADS LRQFHGMSTN 

       310        320 
DLRQRRFDRL MAYGKFKETT PGA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001043 Genomic DNA. Translation: ACC70570.1.
RefSeqYP_001857616.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6242879.
GenomeReviewsGene locus Bphy_1388 in contig CP001043_GR.
KEGGbph:Bphy_1388.

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_BURP8
AccessionPrimary (citable) accession number: B2JIR9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: November 3, 2009
This is version 12 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