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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Nucleophile
Binding sitei105 – 1051SubstrateBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Sitei128 – 1281Important for enzyme activity
Binding sitei212 – 2121SubstrateBy similarity
Active sitei271 – 2711Proton acceptorCurated

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-4890-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341F → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi104 – 1041D → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi105 – 1051R → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi108 – 1081R → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi128 – 1281D → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi147 – 1471Y → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi149 – 1491H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi150 – 1501W → A, F, K, Q, R or Y: Abolishes fluoroacetate dehalogenase activity, but does not abolish activity towards chloroacetate. 1 Publication
Mutagenesisi179 – 1791W → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi212 – 2121Y → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi271 – 2711H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi272 – 2721F → A: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Fluoroacetate dehalogenasePRO_0000398585Add
BLAST

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

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi13 – 2311Combined sources
Beta strandi25 – 317Combined sources
Helixi38 – 414Combined sources
Helixi44 – 485Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 576Combined sources
Helixi75 – 773Combined sources
Helixi79 – 9214Combined sources
Beta strandi96 – 1038Combined sources
Helixi105 – 11612Combined sources
Helixi118 – 1203Combined sources
Beta strandi121 – 1288Combined sources
Helixi132 – 1376Combined sources
Helixi141 – 1466Combined sources
Helixi149 – 1524Combined sources
Helixi159 – 1668Combined sources
Helixi168 – 17710Combined sources
Turni178 – 1803Combined sources
Helixi184 – 1863Combined sources
Helixi189 – 19911Combined sources
Helixi202 – 21514Combined sources
Helixi218 – 2258Combined sources
Turni226 – 2283Combined sources
Beta strandi235 – 2406Combined sources
Helixi244 – 2485Combined sources
Helixi251 – 2555Combined sources
Helixi256 – 2583Combined sources
Beta strandi259 – 26911Combined sources
Helixi273 – 2764Combined sources
Helixi278 – 29316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y37X-ray1.50A/B1-304[»]
3B12X-ray1.20A/B1-304[»]
ProteinModelPortaliQ1JU72.
SMRiQ1JU72. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1JU72.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1502Substrate bindingBy similarity

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y37X-ray1.50A/B1-304[»]
3B12X-ray1.20A/B1-304[»]
ProteinModelPortaliQ1JU72.
SMRiQ1JU72. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERibursp-deha. Haloacetate_dehalogenase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-4890-MONOMER.
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: October 14, 2015
This is version 37 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.