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Reviewed, UniProtKB/Swiss-Prot Q57HM7 (FADA_SALCH)

Last modified February 9, 2010. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant 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: SCH_3879
OrganismSalmonella choleraesuis [Complete proteome] [HAMAP]
Taxonomic identifier28901 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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. HAMAP MF_01620

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: HAMAP

lipid catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3873873-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000206388

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q57HM7-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 66671F49E70EA83A

FASTA38741,034
        10         20         30         40         50         60 
MEQVVIVDAI RTPMGRSKGG AFRNERAEDL 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 LKQFNYDEVI 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]"The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
Nucleic Acids Res. 33:1690-1698(2005) [PubMed: 15781495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC-B67.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017220 Genomic DNA. Translation: AAX67785.1.
RefSeqYP_218866.1.

3D structure databases

SMRQ57HM7. Positions 4-387.
ModBaseSearch...

Genome annotation databases

GeneID3336413.
GenomeReviewsGene locus SCH_3879 in contig AE017220_GR.
KEGGsec:SC3879.
NMPDRfig|321314.4.peg.3208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG370930.
OMAAIDDIYW.

Enzyme and pathway databases

BioCycSENT321314:SCH_3879-MONOMER.
BRENDA2.3.1.16. 276841.

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.
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_SALCH
AccessionPrimary (citable) accession number: Q57HM7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: May 10, 2005
Last modified: February 9, 2010
This is version 39 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents