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Protein

3-ketoacyl-CoA thiolase

Gene

fadI

Organism
Shewanella baltica (strain OS185)
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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processFatty 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:Shew185_2781
OrganismiShewanella baltica (strain OS185)
Taxonomic identifieri402882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000695081 – 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

ProteinModelPortaliA6WQ26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000012240.
KOiK00632.
OMAiMTAFPEP.

Family and domain databases

CDDicd00751. thiolase. 1 hit.
Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01618. FadI. 1 hit.
InterProiView protein in InterPro
IPR012806. Ac-CoA_C-AcTrfase_FadI.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
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
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.

Sequencei

Sequence statusi: Complete.

A6WQ26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDRQQVTNA KGERIAIVAG LRTPFAKQAT AFHGVSALDM GKMVVNELLA
60 70 80 90 100
RSELDPKLIE QLVYGQVVQM PAAPNIAREI VLGTGMNVST DAYSVTRACA
110 120 130 140 150
TSFQSAVNVA ESIMTGNIEI GIAGGADSSS VLPIGVSKKL AHALVDLNKA
160 170 180 190 200
RSFGQKLQIF RRLGIKDLLP VPPAVAEYST GLSMGQTAEQ MAKTYNISRA
210 220 230 240 250
DQDALAHRSH TLASETWASG HLRDEVMVAH VPPYKQFIDR DNNIRENSVL
260 270 280 290 300
ESYAKLRPAF DKQHGTVTAA NSTPLTDGAS AIILMSEGRA KALGYQPIGY
310 320 330 340 350
IKSYAFSAID VWQDMLMGPS YATPLALKRA GMELEDLTLI EMHEAFAAQT
360 370 380 390 400
LANMQMFASK KFAEEKLGRN RAIGEIDMSK FNVLGGSLAY GHPFAATGTR
410 420 430
LITQVCRELK RRGGGTGLTT ACAAGGLGVA MILEVE
Length:436
Mass (Da):46,764
Last modified:August 21, 2007 - v1
Checksum:i17B5A79C417CD4AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS08915.1.
RefSeqiWP_012089601.1. NC_009665.1.

Genome annotation databases

EnsemblBacteriaiABS08915; ABS08915; Shew185_2781.
KEGGisbm:Shew185_2781.

Similar proteinsi

Entry informationi

Entry nameiFADI_SHEB8
AccessioniPrimary (citable) accession number: A6WQ26
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: October 25, 2017
This is version 70 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families