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A4STF3 (FADA_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase

EC=2.3.1.16
Alternative name(s):
Fatty acid oxidation complex subunit beta
Beta-ketothiolase
Acetyl-CoA acyltransferase
Gene names
Name:fadA
Ordered Locus Names:ASA_4251
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

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_0000292885

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A4STF3-1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 8B2FDB2583A0695D

FASTA38740,976
        10         20         30         40         50         60 
MKDVVIVDCI RTPMGRSKGG AFRNVRAEDL SAHLMSSILL RNPNLDPNEI EDIYWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NAALLAGIPK QVGAVTVNRL CGSSMQALHD ASRAIQVGDG DIFIIGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV DFHPGMAKSV AKASGMMGLT AEMLGKLHGI SRQQQDEFAA RSHRRAYAAT 

       190        200        210        220        230        240 
VEGRFAREIV GLEGHDASGA RFFYDYDEVI RPETTVETLS QLRPVFDPVN GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGASAMLV MSADRAKALG LTPRVRVRSM AVAGCDAAIM GYGPVPATQK ALKRAGLTIG 

       310        320        330        340        350        360 
DIDLVELNEA FAAQSLPCVK DLGLLDVAEE KVNLNGGAIA LGHPLGCSGS RISTTLIHLM 

       370        380 
EEKDANLGLA TMCIGLGQGI ATVFERV 

« Hide

References

[1]"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449."
Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO92175.1.
RefSeqYP_001143923.1.

3D structure databases

ProteinModelPortalA4STF3.
SMRA4STF3. Positions 2-387.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4STF3.

Genome annotation databases

GeneID4998358.
GenomeReviewsGene locus ASA_4251 in contig CP000644_GR.
KEGGasa:ASA_4251.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMAAIDDIYW.
PhylomeDBA4STF3.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycASAL382245:ASA_4251-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. 1 hit.
PANTHERPTHR18919. 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_AERS4
AccessionPrimary (citable) accession number: A4STF3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 15, 2007
Last modified: August 10, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families