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Protein

Fluoroacetyl-CoA thioesterase

Gene

flK

Organism
Streptomyces cattleya
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Can not use acetyl-CoA as substrate.2 Publications

Catalytic activityi

Fluoroacetyl-CoA + H2O = fluoroacetate + CoA.2 Publications

Kineticsi

Kcat is 390 sec(-1) with fluoroacetyl-CoA as substrate and 0.06 sec(-1) with acetyl-CoA (at pH 7.6 and 25 degrees Celsius, PubMed:20836570). Kcat is 0.044 sec(-1) with fluoroacetyl-CoA as substrate (PubMed:20430898).1 Publication

Manual assertion based on experiment ini

  1. KM=30 µM for fluoroacetyl-CoA (at pH 8 and 25 degrees Celsius, PubMed:16720268 and PubMed:20430898)3 Publications
  2. KM=8 µM for fluoroacetyl-CoA (at pH 7.6 and 25 degrees Celsius, PubMed:20836570)3 Publications
  3. KM=2.1 mM for acetyl-CoA (at pH 7.6 and 25 degrees Celsius, PubMed:20836570)3 Publications
  1. Vmax=15 µmol/min/mg enzyme with fluoroacetyl-CoA as substrate (at pH 8 and 25 degrees Celsius, PubMed:16720268)3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei421
Active sitei501
Binding sitei69Coenzyme A; via carbonyl oxygen2 Publications1
Binding sitei69Substrate; via amide nitrogen and carbonyl oxygen2 Publications1
Active sitei761
Binding sitei120Substrate2 Publications1

GO - Molecular functioni

  • CoA hydrolase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15928.
BRENDAi3.1.2.29. 5990.

Names & Taxonomyi

Protein namesi
Recommended name:
Fluoroacetyl-CoA thioesterase (EC:3.1.2.29)
Gene namesi
Name:flK
OrganismiStreptomyces cattleya
Taxonomic identifieri29303 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23V → A: Reduced activity. 1 Publication1
Mutagenesisi26L → A: Reduced activity. 1 Publication1
Mutagenesisi33F → A: Reduced activity. 1 Publication1
Mutagenesisi36F → A: Reduced activity. 1 Publication1
Mutagenesisi42T → A: Reduced activity. 2 Publications1
Mutagenesisi42T → C or S: Enhancement of acetyl-CoA binding, but reduced activity toward fluoroacetyl-CoA. 2 Publications1
Mutagenesisi50E → A or Q: Reduced activity and affinity. 2 Publications1
Mutagenesisi76H → A: Reduced activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004191301 – 139Fluoroacetyl-CoA thioesteraseAdd BLAST139

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1139
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 16Combined sources7
Helixi19 – 21Combined sources3
Helixi23 – 26Combined sources4
Helixi31 – 33Combined sources3
Beta strandi38 – 40Combined sources3
Helixi42 – 56Combined sources15
Helixi58 – 60Combined sources3
Beta strandi65 – 75Combined sources11
Beta strandi84 – 96Combined sources13
Beta strandi99 – 107Combined sources9
Beta strandi109 – 124Combined sources16
Helixi125 – 133Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KUVX-ray1.50A/B1-139[»]
3KUWX-ray1.90A/B1-139[»]
3KV7X-ray1.56A/B1-139[»]
3KV8X-ray1.85A/B1-139[»]
3KVIX-ray1.76A/B1-139[»]
3KVUX-ray2.00A/B/C/D1-139[»]
3KVZX-ray2.10A/B/C/D/E/F/G/H1-139[»]
3KW1X-ray1.90A/B/C/D/E/F/G/H1-139[»]
3KX7X-ray1.70A/B1-139[»]
3KX8X-ray2.35A/B/C/D/E/F/G/H1-139[»]
3P2QX-ray1.85A/B1-139[»]
3P2RX-ray2.46A/B1-139[»]
3P2SX-ray1.95A/B1-139[»]
3P3FX-ray2.30A/B/C/D/E/F1-139[»]
3P3IX-ray2.00A/B/C/D/E/F1-139[»]
ProteinModelPortaliQ1EMV2.
SMRiQ1EMV2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1EMV2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 50Substrate bindingAdd BLAST11
Regioni76 – 77Coenzyme A binding2

Phylogenomic databases

eggNOGiENOG4105KIP. Bacteria.
COG5496. LUCA.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR025540. FlK.
IPR029069. HotDog_dom.
[Graphical view]
PIRSFiPIRSF014972. FlK. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1EMV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDGMRVGER FTHDFVVPPH KTVRHLYPES PEFAEFPEVF ATGFMVGLME
60 70 80 90 100
WACVRAMAPY LEPGEGSLGT AICVTHTAAT PPGLTVTVTA ELRSVEGRRL
110 120 130
SWRVSAHDGV DEIGSGTHER AVIHLEKFNA KVRQKTPAG
Length:139
Mass (Da):15,257
Last modified:July 11, 2006 - v1
Checksum:iC32DE9465552909C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM055586 Genomic DNA. Translation: CAJ20012.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM055586 Genomic DNA. Translation: CAJ20012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KUVX-ray1.50A/B1-139[»]
3KUWX-ray1.90A/B1-139[»]
3KV7X-ray1.56A/B1-139[»]
3KV8X-ray1.85A/B1-139[»]
3KVIX-ray1.76A/B1-139[»]
3KVUX-ray2.00A/B/C/D1-139[»]
3KVZX-ray2.10A/B/C/D/E/F/G/H1-139[»]
3KW1X-ray1.90A/B/C/D/E/F/G/H1-139[»]
3KX7X-ray1.70A/B1-139[»]
3KX8X-ray2.35A/B/C/D/E/F/G/H1-139[»]
3P2QX-ray1.85A/B1-139[»]
3P2RX-ray2.46A/B1-139[»]
3P2SX-ray1.95A/B1-139[»]
3P3FX-ray2.30A/B/C/D/E/F1-139[»]
3P3IX-ray2.00A/B/C/D/E/F1-139[»]
ProteinModelPortaliQ1EMV2.
SMRiQ1EMV2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105KIP. Bacteria.
COG5496. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15928.
BRENDAi3.1.2.29. 5990.

Miscellaneous databases

EvolutionaryTraceiQ1EMV2.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR025540. FlK.
IPR029069. HotDog_dom.
[Graphical view]
PIRSFiPIRSF014972. FlK. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFLK_STRCT
AccessioniPrimary (citable) accession number: Q1EMV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: July 11, 2006
Last modified: November 2, 2016
This is version 32 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.