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B5FNX7 (B5FNX7_SALDC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase HAMAP MF_01620
EC=2.3.1.16 HAMAP MF_01620
Alternative name(s):
Acetyl-CoA acyltransferase HAMAP MF_01620
Beta-ketothiolase HAMAP MF_01620
Fatty acid oxidation complex subunit beta HAMAP MF_01620
Gene names
Name:fadA HAMAP MF_01620
Ordered Locus Names:SeD_A4368
OrganismSalmonella dublin (strain CT_02021853) [Complete proteome] [HAMAP] EMBL ACH75380.1
Taxonomic identifier439851 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella dublin

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 SAAS SAAS020613

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620 SAAS SAAS020613

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01620 SAAS SAAS020613

Subcellular location

Cytoplasm By similarity HAMAP MF_01620.

Sequence similarities

Belongs to the thiolase family. HAMAP MF_01620

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site911Acyl-thioester intermediate By similarity HAMAP MF_01620
Active site3431Proton acceptor By similarity HAMAP MF_01620
Active site3731Proton acceptor By similarity HAMAP MF_01620

Sequences

Sequence LengthMass (Da)Tools
B5FNX7 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 9503B4E83617B40C

FASTA38740,977
        10         20         30         40         50         60 
MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPSLTAATL DDIYWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NAALLAEIPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QVCLVGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLSRLHGI SREMQDQFAA RSHARAWAAT 

       190        200        210        220        230        240 
QSGAFKTEII PTGGHDADGV LKQFSYDEVI RPETTVEALS TLRPAFDPVS GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGAAAMLV MSESRARELG LKPRARIRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS 

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

       370        380 
ERKDAQFGLA TMCIGLGQGI ATVFERV

« Hide

References

[1]"Complete genome of Salmonella dublin strain CT_02021853."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001144 Genomic DNA. Translation: ACH75380.1.
RefSeqYP_002217908.1. NC_011205.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB5FNX7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6872006.
GenomeReviewsGene locus SeD_A4368 in contig CP001144_GR.
KEGGsed:SeD_A4368.
PATRIC18496800. VBISalEnt111443_4292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG370930.
OMAAIDDIYW.
ProtClustDBPRK08947.

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 nameB5FNX7_SALDC
AccessionPrimary (citable) accession number: B5FNX7
Entry history
Integrated into UniProtKB/TrEMBL: October 14, 2008
Last sequence update: October 14, 2008
Last modified: December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info