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Reviewed, UniProtKB/Swiss-Prot Q5WEF5 (ACCA_BACSK)

Last modified February 9, 2010. Version 35. 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: ABC2720
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
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. HAMAP MF_00823

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. HAMAP MF_00823

Subcellular location

Cytoplasm By similarity HAMAP MF_00823.

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 – 324324Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_0000223732

Sequences

Sequence LengthMass (Da)Tools
Q5WEF5-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9157523BA33B8E7F

FASTA32436,158
        10         20         30         40         50         60 
MSSEQEFEKP VIELRQKIAD LRAFAMERDM DLSTEIKKME ARLSELEEEV YANLQPWERV 

        70         80         90        100        110        120 
QIARDHERPT TLDYVDVLFE DFLEMHGDRL FGDDKAIVGG IATYKGKPVT VIGHQRGKDT 

       130        140        150        160        170        180 
KENIVRYFGS PHPEGYRKAL RLMKQAEKFK RPIICFIDTK GAYPGKAAEE RGQSEAIARN 

       190        200        210        220        230        240 
LLEMAGLKVP TISIVIGEGG SGGALALGVA DEIHMLENAT YSVISPEGAA AILWKDAGKA 

       250        260        270        280        290        300 
KKAAESMRIT APDLYELGII DSIIPEPRGG AQRNLHQQAD EIDRLLEKAL TRLAEKPVDV 

       310        320 
LLDERYEKFM KIGHIPEEAA TTGQ 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD65255.1.
RefSeqYP_176216.1.

3D structure databases

SMRQ5WEF5. Positions 6-313.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WEF5.

Genome annotation databases

GeneID3203524.
GenomeReviewsGene locus ABC2720 in contig AP006627_GR.
KEGGbcl:ABC2720.
NMPDRfig|66692.3.peg.3061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0825.
HOGENOMHBG286557.
OMAHSVYTVA.

Enzyme and pathway databases

BioCycBCLA66692:ABC2720-MONOMER.

Family and domain databases

HAMAPMF_00823. AcetylCoA_CT_alpha.
[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_BACSK
AccessionPrimary (citable) accession number: Q5WEF5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 23, 2004
Last modified: February 9, 2010
This is version 35 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