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Reviewed, UniProtKB/Swiss-Prot Q65G81 (ACCA_BACLD)

Last modified November 3, 2009. Version 37. 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: BLi03069, BL00404
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length325 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 – 325325Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_0000223734

Sequences

Sequence LengthMass (Da)Tools
Q65G81-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 8B99948996E73F14

FASTA32536,399
        10         20         30         40         50         60 
MAGELEFEKP VVELREKISE LKKFTQDSDM DLSSEITKLE ARLERLEEDI YTNLKAWDRV 

        70         80         90        100        110        120 
QIARHPNRPT TLDYIEHLFT DFFECHGDRY FGDDEAIVGG IAKFRGLPVT VIGQQRGKDT 

       130        140        150        160        170        180 
KENIRRNFGM PHPEGYRKAL RLMKQADKFN RPIICFIDTK GAYPGKAAEE RGQSEAIAKN 

       190        200        210        220        230        240 
LFEMAGLSVP VISIVIGEGG SGGALALGVA NRLLMLENST YSVISPEGAA AILWKDSGLA 

       250        260        270        280        290        300 
KKAAETMKIT APDLKELDII DHVIKEVRGG AHRDVEQQAA YIDEALKGEL KSLLKLDKNE 

       310        320 
LIQQRYNKYK SIGKISTENQ YVGIK 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017333 Genomic DNA. Translation: AAU41933.1.
CP000002 Genomic DNA. Translation: AAU24574.1.
RefSeqYP_080212.1.
YP_092626.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ65G81.

Genome annotation databases

GeneID3028933.
3098677.
GenomeReviewsGene locus BLi03069 in contig AE017333_GR.
Gene locus BL00404 in contig CP000002_GR.
KEGGbld:BLi03069.
bli:BL00404.
NMPDRfig|279010.5.peg.3431.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ65G81.
OMAHSVYTVA.

Enzyme and pathway databases

BioCycBLIC279010:BL00404-MON.

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_BACLD
AccessionPrimary (citable) accession number: Q65G81
Secondary accession number(s): Q62RN6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 37 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