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Protein

3-ketoacyl-CoA thiolase

Gene

fadI

Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processFatty acid metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

UniPathwayi
UPA00659

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:ECP_2380
OrganismiEscherichia coli O6:K15:H31 (strain 536 / UPEC)
Taxonomic identifieri362663 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000694981 – 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

ProteinModelPortaliQ0TFA5
SMRiQ0TFA5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CHU Bacteria
COG0183 LUCA
HOGENOMiHOG000012240
KOiK00632
OMAiMTAFPEP

Family and domain databases

CDDicd00751 thiolase, 1 hit
Gene3Di3.40.47.10, 1 hit
HAMAPiMF_01618 FadI, 1 hit
InterProiView protein in InterPro
IPR012806 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
PANTHERiPTHR18919:SF113 PTHR18919:SF113, 1 hit
PfamiView protein in Pfam
PF02803 Thiolase_C, 1 hit
PF00108 Thiolase_N, 1 hit
PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
SUPFAMiSSF53901 SSF53901, 2 hits
TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
TIGR02446 FadI, 1 hit
PROSITEiView protein in PROSITE
PS00098 THIOLASE_1, 1 hit
PS00737 THIOLASE_2, 1 hit
PS00099 THIOLASE_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q0TFA5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQVLPLVTR QGDRIAIVSG LRTPFARQAT AFHGIPAVDL GKMVVGELLA
60 70 80 90 100
RTEIPAEVIE QLVFGQVVQM PEAPNIAREI VLGTGMNVHT DAYSVSRACA
110 120 130 140 150
TSFQAVANVA ESLMAGTIRA GIAGGADSSS VLPIGVSKKL ARVLVDVNKA
160 170 180 190 200
RTMSQRLKLF SRLRLRDLMP VPPAVAEYST GLRMGDTAEQ MAKTYGITRE
210 220 230 240 250
QQDALAHRSH QRAAQAWSEG KLKEEVMTAF IPPYKQPLVE DNNIRGNSSL
260 270 280 290 300
ADYAKLRPAF DRKHGTVTAA NSTPLTDGAA AVILMTESRA KELGLVPLGY
310 320 330 340 350
LRSYAFTAID VWQDMLLGPA WSTPLALERA GLTMGDLTLI DMHEAFAAQT
360 370 380 390 400
LANIQLLGSE RFARDVLGRA HATGEVDESK FNVLGGSIAY GHPFAATGAR
410 420 430
MITQTLHELR RRGGGFGLVT ACAAGGLGAA MVLEAE
Length:436
Mass (Da):46,557
Last modified:September 5, 2006 - v1
Checksum:i3C3B8DDE296C3E3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000247 Genomic DNA Translation: ABG70374.1
RefSeqiWP_000531977.1, NC_008253.1

Genome annotation databases

EnsemblBacteriaiABG70374; ABG70374; ECP_2380
KEGGiecp:ECP_2380

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000247 Genomic DNA Translation: ABG70374.1
RefSeqiWP_000531977.1, NC_008253.1

3D structure databases

ProteinModelPortaliQ0TFA5
SMRiQ0TFA5
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG70374; ABG70374; ECP_2380
KEGGiecp:ECP_2380

Phylogenomic databases

eggNOGiENOG4105CHU Bacteria
COG0183 LUCA
HOGENOMiHOG000012240
KOiK00632
OMAiMTAFPEP

Enzyme and pathway databases

UniPathwayi
UPA00659

Family and domain databases

CDDicd00751 thiolase, 1 hit
Gene3Di3.40.47.10, 1 hit
HAMAPiMF_01618 FadI, 1 hit
InterProiView protein in InterPro
IPR012806 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
PANTHERiPTHR18919:SF113 PTHR18919:SF113, 1 hit
PfamiView protein in Pfam
PF02803 Thiolase_C, 1 hit
PF00108 Thiolase_N, 1 hit
PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
SUPFAMiSSF53901 SSF53901, 2 hits
TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
TIGR02446 FadI, 1 hit
PROSITEiView protein in PROSITE
PS00098 THIOLASE_1, 1 hit
PS00737 THIOLASE_2, 1 hit
PS00099 THIOLASE_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFADI_ECOL5
AccessioniPrimary (citable) accession number: Q0TFA5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: October 10, 2018
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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