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Protein

3-ketoacyl-CoA thiolase

Gene

fadI

Organism
Vibrio fischeri (strain ATCC 700601 / ES114)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051Acyl-thioester intermediateUniRule annotation
Active sitei398 – 3981Proton acceptorUniRule annotation
Active sitei428 – 4281Proton acceptorUniRule annotation

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

BioCyciAFIS312309:GIWP-1915-MONOMER.
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:VF_1811
OrganismiVibrio fischeri (strain ATCC 700601 / ES114)
Taxonomic identifieri312309 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
Proteomesi
  • UP000000537 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4424423-ketoacyl-CoA thiolasePRO_0000206450Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi312309.VF_1811.

Structurei

3D structure databases

ProteinModelPortaliQ5E3U0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012240.
KOiK00632.
OMAiMTAFPEP.
OrthoDBiEOG68SVWR.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
HAMAPiMF_01618. FadI.
InterProiIPR012806. Ac-CoA_C-AcTrfase_FadI.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
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.
PROSITEiPS00737. THIOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5E3U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSVNSSKY QPLTTRQGDR IAVVSGIRTP FAKQSTAFST TPAVDLGKLA
60 70 80 90 100
VKALMDKTDI DPKLIDQVVF GQVVQMPEAP NIAREIVLGT GMNIGTDAYS
110 120 130 140 150
VTRACATSFQ TTANVVESIM AGTIDIGIAG GADSSSVLPI GVSKKLASTL
160 170 180 190 200
LALSKTKTVY QKLSLLRTLS LKDIAPVPPA VAEYSTGISM GQTAEQMAKS
210 220 230 240 250
HGITREEQDA LAHRSHTLAA KAWKDGLIQD EVMTAFPEPY TAWLDHDNNI
260 270 280 290 300
RHDSDLASYA KLRPAFDHKY GSVTAANSTP LTDGGAALLL MSEKRAKELG
310 320 330 340 350
YEPLGYIRSF AFSAIDVHHD MLMGPSYATP MALDKAGISL SDLTLIDMHE
360 370 380 390 400
AFAAQTLSNV KMFASNKFAK EYLGRDKAIG EIDMEKFNVL GGSIAYGHPF
410 420 430 440
AATGARMIIQ TLRELKRRGG GLGLNTACAA GGLGAAMVLE VE
Length:442
Mass (Da):47,077
Last modified:March 15, 2005 - v1
Checksum:i1E8947E33B4C2FAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000020 Genomic DNA. Translation: AAW86306.1.
RefSeqiWP_011262340.1. NC_006840.2.
YP_205194.1. NC_006840.2.

Genome annotation databases

EnsemblBacteriaiAAW86306; AAW86306; VF_1811.
GeneIDi3279084.
KEGGivfi:VF_1811.
PATRICi20114316. VBIVibFis127983_1839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000020 Genomic DNA. Translation: AAW86306.1.
RefSeqiWP_011262340.1. NC_006840.2.
YP_205194.1. NC_006840.2.

3D structure databases

ProteinModelPortaliQ5E3U0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi312309.VF_1811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW86306; AAW86306; VF_1811.
GeneIDi3279084.
KEGGivfi:VF_1811.
PATRICi20114316. VBIVibFis127983_1839.

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012240.
KOiK00632.
OMAiMTAFPEP.
OrthoDBiEOG68SVWR.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciAFIS312309:GIWP-1915-MONOMER.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
HAMAPiMF_01618. FadI.
InterProiIPR012806. Ac-CoA_C-AcTrfase_FadI.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
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.
PROSITEiPS00737. THIOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700601 / ES114.

Entry informationi

Entry nameiFADI_VIBF1
AccessioniPrimary (citable) accession number: Q5E3U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 15, 2005
Last modified: November 11, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.