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A7GWR2 (ACCA_CAMC5) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. 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:Ccur92_03500
ORF Names:CCV52592_1910
OrganismCampylobacter curvus (strain 525.92) [Complete proteome] [HAMAP]
Taxonomic identifier360105 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length311 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
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 – 311311Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000062597

Sequences

Sequence LengthMass (Da)Tools
A7GWR2 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: DE618840D09F8EF8

FASTA31134,500
        10         20         30         40         50         60 
MSSYLDFEKS IKQIDDDIAN ARIKGDEHAV EILNKNLEKE VAKVYKNLNE YQRLQLARHP 

        70         80         90        100        110        120 
DRPYAIDYIR SFLMDAYEIH GDRAFRDDPA IVCYVGYIGG KKAMVIGEQK GRGTKNKLRR 

       130        140        150        160        170        180 
NFGMPHPEGY RKALRVAKLA EKFNLPILFL IDTPGAYPGV GAEERGQSEA IARNLFEFAN 

       190        200        210        220        230        240 
LKVPTIAVVI GEGGSGGALA IGVADKLAMM KNSVFSVISP EGCAAILWND PSKQEQATKA 

       250        260        270        280        290        300 
MKITADDLKN LKLIDDVIKE PINGAHRDKD GAAKELASYF VSKLEKLEKL SIDELVAKRI 

       310 
DKILSVGAYE E 

« Hide

References

[1]"Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 525.92.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000767 Genomic DNA. Translation: EAT99424.2.
RefSeqYP_001407654.1. NC_009715.1.

3D structure databases

ProteinModelPortalA7GWR2.
SMRA7GWR2. Positions 1-311.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GWR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5407440.
GenomeReviewsGene locus Ccur92_03500 in contig CP000767_GR.
KEGGccv:CCV52592_1910.
PATRIC20031110. VBICamCur47627_0375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0825.
HOGENOMHBG286557.
OMAGRDTKDN.
ProtClustDBPRK05724.

Enzyme and pathway databases

BioCycCCUR360105:CCV52592_1910-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_CAMC5
AccessionPrimary (citable) accession number: A7GWR2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 34 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