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Q9PI62 (ACCA_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 alpha

Short name=ACCase subunit alpha
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha
EC=6.4.1.2
Gene names
Name:accA
Ordered Locus Names:Cj0443
OrganismCampylobacter jejuni
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length312 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.

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
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_0000223747

Sequences

Sequence LengthMass (Da)Tools
Q9PI62 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8DDE111C042DADA4

FASTA31234,253
        10         20         30         40         50         60 
MASYLDFEKN IQQIDEDIIN AQIKGDTEAV SILKKNLEKE ISKTYKNLSD FQRLQLARHP 

        70         80         90        100        110        120 
DRPYALDYIE LILNDAHEIH GDRAFRDDPA IVCFMGYLGE KKIIVIGEQK GRGTKDKIAR 

       130        140        150        160        170        180 
NFGMPHPEGY RKALRVAGLA EKFQIPILFL IDTPGAYPGI GAEERGQSEA IARNLYELSD 

       190        200        210        220        230        240 
LKIPTIAIVI GEGGSGGALA IGVADKLAMM KNSVFSVISP EGCAAILWND PAKSEAATKA 

       250        260        270        280        290        300 
MKVTADDLKS QGLIDDVIDE PTNGAHRNKE AAAVAIADYV KKSLNELENI DVRELSANRM 

       310 
QKILKLGAYQ EA 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34593.1.
PIRA81389.
RefSeqYP_002343880.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PI62.
SMRQ9PI62. Positions 1-311.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PI62. 37 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID904768.
GenomeReviewsGene locus Cj0443 in contig AL111168_GR.
KEGGcje:Cj0443.
PATRIC20057811. VBICamJej33762_0434.

Phylogenomic databases

HOGENOMHBG286557.
OMAGRDTKDN.
ProtClustDBPRK05724.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0443-MONOMER.

Family and domain databases

HAMAPMF_00823. AcetylCoA_CT_alpha.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR011763. COA_CT_C.
[Graphical view]
KOK01962.
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_CAMJE
AccessionPrimary (citable) accession number: Q9PI62
Secondary accession number(s): Q0PB67
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families