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Q9F0Y6 (FADA_ENTCL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 50. 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
OrganismEnterobacter cloacae
Taxonomic identifier550 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

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
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_0000206370

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q9F0Y6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5277420310B8067F

FASTA38740,808
        10         20         30         40         50         60 
MEKVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALDPAAL DDIYWGCLHQ 

        70         80         90        100        110        120 
TLEQGFNLAR NASLLAEIPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV HFHPGMSRNV AKAAGMMGLT AEMLSRLHGI SREMQDAFAA RSHARAWAAT 

       190        200        210        220        230        240 
QSGAFKNEII PTGGHDADGV LKQFSYDEVI RPETTVEALS TLRPAFDPVT GTVTAGTSSA 

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

       310        320        330        340        350        360 
DIDLFEMNEA FAAQILPCIK DLGLMGQIDE KINLNGGAIA LGHPLGCSGA RISTTLINLM 

       370        380 
EGKDAQFGLA TMCIGLGQGI ATVFERV 

« Hide

References

[1]"Fatty acid competition as a mechanism by which Enterobacter cloacae suppresses Pythium ultimum sporangium germination and damping-off."
van Dijk K., Nelson E.B.
Appl. Environ. Microbiol. 66:5340-5347(2000) [PubMed: 11097912] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A-11 / 501R3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF191029 Genomic DNA. Translation: AAG17184.1.

3D structure databases

ProteinModelPortalQ9F0Y6.
SMRQ9F0Y6. Positions 4-387.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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_ENTCL
AccessionPrimary (citable) accession number: Q9F0Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2001
Last modified: May 31, 2011
This is version 50 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