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A6GX95 (ACCA_FLAPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:FP0613
OrganismFlavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)
Taxonomic identifier402612 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium

Protein attributes

Sequence length317 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 – 317317Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000072882

Sequences

Sequence LengthMass (Da)Tools
A6GX95 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 5B51F85CF843666E

FASTA31735,769
        10         20         30         40         50         60 
MEYLDFELPI KELLEQLDKC QIIGTESNVD VTETCKQISQ KLEDTKKDIY GNLTAWQRVQ 

        70         80         90        100        110        120 
LSRHPSRPYT LEHITNLTKG TFLELFGDRN FKDDKAMIGG LGKIGDQSFM FVGQQKGINT 

       130        140        150        160        170        180 
KMRQFRNFGM PNPEGYRKAL RLMKMAEKFN IPVVTLIDTP GAFPGIEAEE RGQGEAIARN 

       190        200        210        220        230        240 
ILEMARLKVP IICVIIGEGA SGGALGIGVG DRVLMMENTW YSVISPESCS SILWKSWEYK 

       250        260        270        280        290        300 
EQAAEALKLT SADMKRQKIV DDIIPEPLGG AHYDKATAFK TVEEYILKAF NELKDLSTTD 

       310 
LVAQRMDKYS KMGEYNE 

« Hide

References

[1]"Complete genome sequence of the fish pathogen Flavobacterium psychrophilum."
Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B., Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F., Claverol S., Dumetz F., Le Henaff M., Benmansour A.
Nat. Biotechnol. 25:763-769(2007) [PubMed: 17592475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JIP02/86 / ATCC 49511.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM398681 Genomic DNA. Translation: CAL42718.1.
RefSeqYP_001295534.1. NC_009613.1.

3D structure databases

ProteinModelPortalA6GX95.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6GX95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5300636.
GenomeReviewsGene locus FP0613 in contig AM398681_GR.
KEGGfps:FP0613.
NMPDRfig|402612.4.peg.606.
PATRIC21906090. VBIFlaPsy4505_0626.

Phylogenomic databases

eggNOGCOG0825.
HOGENOMHBG286557.
OMAGRDTKDN.
ProtClustDBPRK05724.

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_FLAPJ
AccessionPrimary (citable) accession number: A6GX95
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 24, 2007
Last modified: December 14, 2011
This is version 33 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