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Protein

Fluoroacetate dehalogenase

Gene

fac-dex

Organism
Burkholderia sp.
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic defluorination of fluoroacetate to produce glycolate. Has only very low activity towards chloroacetate.2 Publications

Catalytic activityi

Haloacetate + H2O = glycolate + halide.2 Publications

Kineticsi

  1. KM=9.1 mM for fluoroacetate2 Publications
  1. Vmax=61 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 8.5-9.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei104Nucleophile1
Binding sitei105SubstrateBy similarity1
Binding sitei108SubstrateBy similarity1
Sitei128Important for enzyme activity1
Binding sitei212SubstrateBy similarity1
Active sitei271Proton acceptorCurated1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.8.1.3. 1033.

Protein family/group databases

ESTHERibursp-deha. Haloacetate_dehalogenase.

Names & Taxonomyi

Protein namesi
Recommended name:
Fluoroacetate dehalogenase (EC:3.8.1.3)
Gene namesi
Name:fac-dex
OrganismiBurkholderia sp.
Taxonomic identifieri36773 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34F → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi104D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi105R → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi108R → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi128D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi147Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi149H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi150W → A, F, K, Q, R or Y: Abolishes fluoroacetate dehalogenase activity, but does not abolish activity towards chloroacetate. 1 Publication1
Mutagenesisi179W → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi212Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi271H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi272F → A: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003985851 – 304Fluoroacetate dehalogenaseAdd BLAST304

Expressioni

Inductioni

Up-regulated by fluoroacetate. Not detectable in the absence of fluoroacetate, or when cells are grown on Luria broth.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi13 – 23Combined sources11
Beta strandi25 – 31Combined sources7
Helixi38 – 41Combined sources4
Helixi44 – 48Combined sources5
Turni49 – 51Combined sources3
Beta strandi52 – 57Combined sources6
Helixi75 – 77Combined sources3
Helixi79 – 92Combined sources14
Beta strandi96 – 103Combined sources8
Helixi105 – 116Combined sources12
Helixi118 – 120Combined sources3
Beta strandi121 – 128Combined sources8
Helixi132 – 137Combined sources6
Helixi141 – 146Combined sources6
Helixi149 – 152Combined sources4
Helixi159 – 166Combined sources8
Helixi168 – 177Combined sources10
Turni178 – 180Combined sources3
Helixi184 – 186Combined sources3
Helixi189 – 199Combined sources11
Helixi202 – 215Combined sources14
Helixi218 – 225Combined sources8
Turni226 – 228Combined sources3
Beta strandi235 – 240Combined sources6
Helixi244 – 248Combined sources5
Helixi251 – 255Combined sources5
Helixi256 – 258Combined sources3
Beta strandi259 – 269Combined sources11
Helixi273 – 276Combined sources4
Helixi278 – 293Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y37X-ray1.50A/B1-304[»]
3B12X-ray1.20A/B1-304[»]
ProteinModelPortaliQ1JU72.
SMRiQ1JU72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1JU72.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 151AB hydrolase-1Sequence analysisAdd BLAST126

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 150Substrate bindingBy similarity2

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1JU72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEGFERRLV DVGDVTINCV VGGSGPALLL LHGFPQNLHM WARVAPLLAN
60 70 80 90 100
EYTVVCADLR GYGGSSKPVG APDHANYSFR AMASDQRELM RTLGFERFHL
110 120 130 140 150
VGHDRGGRTG HRMALDHPDS VLSLAVLDII PTYVMFEEVD RFVARAYWHW
160 170 180 190 200
YFLQQPAPYP EKVIGADPDT FYEGCLFGWG ATGADGFDPE QLEEYRKQWR
210 220 230 240 250
DPAAIHGSCC DYRAGGTIDF ELDHGDLGRQ VQCPALVFSG SAGLMHSLFE
260 270 280 290 300
MQVVWAPRLA NMRFASLPGG HFFVDRFPDD TARILREFLS DARSGIHQTE

RRES
Length:304
Mass (Da):34,087
Last modified:June 13, 2006 - v1
Checksum:i0EE1B70133C7F8F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB259121 Genomic DNA. Translation: BAE94252.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB259121 Genomic DNA. Translation: BAE94252.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y37X-ray1.50A/B1-304[»]
3B12X-ray1.20A/B1-304[»]
ProteinModelPortaliQ1JU72.
SMRiQ1JU72.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERibursp-deha. Haloacetate_dehalogenase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.8.1.3. 1033.

Miscellaneous databases

EvolutionaryTraceiQ1JU72.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDEHA_BURSP
AccessioniPrimary (citable) accession number: Q1JU72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 13, 2006
Last modified: November 2, 2016
This is version 39 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, Direct protein sequencing

Documents

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