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A4WFX5 (FADA_ENT38) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:
3-ketoacyl-CoA thiolase

EC=2.3.1.16
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta
Gene names
Name:fadA
Ordered Locus Names:Ent638_3950
OrganismEnterobacter sp. (strain 638) [Complete proteome] [HAMAP]
Taxonomic identifier399742 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP MF_01620

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_01620.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3873873-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000323544

Sites

Active site911Acyl-thioester intermediate By similarity
Active site3431Proton acceptor By similarity
Active site3731Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WFX5 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: BA35045BFA3417AB

FASTA38741,187
        10         20         30         40         50         60 
MEKVVIVDAI RTPMGRSKGG AFRHVRAEDL SAHLMRSLLA RNPALEASAI DDIYWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NASLLAEIPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QVCMVGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV DFHPGMSRNV AKAAGMMGLT AEMLSRMHGI SREMQDQFAA RSHARAWAAT 

       190        200        210        220        230        240 
QSGAFKNEIL PTGGHDVDGV LKQYYYDEVI RPETTVEALS ALRPAFDPVT GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGAAAMLV MSESRARELG LTPRARIRSM AVVGCDPSIM GYGPVPASKL ALKKAGLTAS 

       310        320        330        340        350        360 
EIDVFEMNEA FAAQILPCIK DLGLMEQIDE KINLNGGAIA LGHPLGCSGA RISTTLINLM 

       370        380 
ERKDAQFGLA TMCIGLGQGI ATVFERV 

« Hide

References

[1]"Complete sequence of chromosome of Enterobacter sp. 638."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000653 Genomic DNA. Translation: ABP62605.1.
RefSeqYP_001178656.1. NC_009436.1.

3D structure databases

ProteinModelPortalA4WFX5.
SMRA4WFX5. Positions 4-387.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WFX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5114670.
GenomeReviewsGene locus Ent638_3950 in contig CP000653_GR.
KEGGent:Ent638_3950.
NMPDRfig|399742.4.peg.3751.
PATRIC20417661. VBIEntSp101211_4114.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMAAIDDIYW.
PhylomeDBA4WFX5.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycESP42895:ENT638_3950-MONOMER.

Family and domain databases

HAMAPMF_01620. FadA.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KOK00632.
PANTHERPTHR18919:SF35. PTHR18919:SF35. 1 hit.
PTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. FadA. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADA_ENT38
AccessionPrimary (citable) accession number: A4WFX5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 39 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