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Protein

3-ketoacyl-CoA thiolase

Gene

fadI

Organism
Salmonella heidelberg (strain SL476)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.UniRule annotation

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei99Acyl-thioester intermediateUniRule annotation1
Active sitei392Proton acceptorUniRule annotation1
Active sitei422Proton acceptorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolaseUniRule annotation (EC:2.3.1.16UniRule annotation)
Alternative name(s):
ACSsUniRule annotation
Acetyl-CoA acyltransferaseUniRule annotation
Acyl-CoA ligaseUniRule annotation
Beta-ketothiolaseUniRule annotation
Fatty acid oxidation complex subunit betaUniRule annotation
Gene namesi
Name:fadIUniRule annotation
Ordered Locus Names:SeHA_C2631
OrganismiSalmonella heidelberg (strain SL476)
Taxonomic identifieri454169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001859741 – 4363-ketoacyl-CoA thiolaseAdd BLAST436

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB4TCA9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000012240.
KOiK00632.
OMAiMTAFPEP.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
HAMAPiMF_01618. FadI. 1 hit.
InterProiIPR012806. Ac-CoA_C-AcTrfase_FadI.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02446. FadI. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4TCA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQALPLVTR QGDRIAIVSG LRTPFARQAT AFHGIPAVDL GKMVVGELLA
60 70 80 90 100
RSEIPADAIE QLVFGQVVQM PEAPNIAREI VLGTGMNVHT DAYSVSRACA
110 120 130 140 150
TSFQAVANVA ESLMAGTIRA GIAGGADSSS VLPIGVSKAL ARVLVDVNKA
160 170 180 190 200
RTTRQRLTLF SRLRLRDLLP VPPAVAEYST GLRMGDTAEQ MAKTYGITRE
210 220 230 240 250
QQDALAHRSH QRAAQAWAEG KLAEEVMTTY VPPYKNPFAE DNNIRGASTL
260 270 280 290 300
ADYAKLRPAF DRKHGSVTAA NSTPLTDGAA AVILMTESRA KELGLRPLGY
310 320 330 340 350
LRSYAFTAID VWQDMLLGPA WSTPLALERA GLTMADLTLF DMHEAFAAQT
360 370 380 390 400
LANLQLLGSE RFACEVLGRA QATGEVDDAK FNVLGGSIAY GHPFAATGAR
410 420 430
MITQTLHELR RRGGGFGLVT ACAAGGLGAA MVLEAE
Length:436
Mass (Da):46,443
Last modified:September 23, 2008 - v1
Checksum:iA76A8D1598559948
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001120 Genomic DNA. Translation: ACF68384.1.
RefSeqiWP_001248122.1. NC_011083.1.

Genome annotation databases

EnsemblBacteriaiACF68384; ACF68384; SeHA_C2631.
KEGGiseh:SeHA_C2631.
PATRICi18512890. VBISalEnt43179_2543.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001120 Genomic DNA. Translation: ACF68384.1.
RefSeqiWP_001248122.1. NC_011083.1.

3D structure databases

ProteinModelPortaliB4TCA9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF68384; ACF68384; SeHA_C2631.
KEGGiseh:SeHA_C2631.
PATRICi18512890. VBISalEnt43179_2543.

Phylogenomic databases

HOGENOMiHOG000012240.
KOiK00632.
OMAiMTAFPEP.

Enzyme and pathway databases

UniPathwayiUPA00659.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
HAMAPiMF_01618. FadI. 1 hit.
InterProiIPR012806. Ac-CoA_C-AcTrfase_FadI.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02446. FadI. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADI_SALHS
AccessioniPrimary (citable) accession number: B4TCA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: November 2, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.