DEHA_BURSP
ID DEHA_BURSP Reviewed; 304 AA.
AC Q1JU72;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Fluoroacetate dehalogenase;
DE EC=3.8.1.3;
GN Name=fac-dex;
OS Burkholderia sp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=36773;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND SUBUNIT.
RC STRAIN=FA1;
RX DOI=10.1016/S1381-1177(03)00098-5;
RA Kurihara T., Yamauchi T., Ichiyama S., Takahata H., Esaki N.;
RT "Purification, characterization, and gene cloning of a novel fluoroacetate
RT dehalogenase from Burkholderia sp. FA1.";
RL J. Mol. Catal., B Enzym. 23:347-355(2003).
RN [2]
RP ACTIVE SITE, AND ENZYME MECHANISM.
RX PubMed=19551770; DOI=10.1002/chem.200801813;
RA Kamachi T., Nakayama T., Shitamichi O., Jitsumori K., Kurihara T.,
RA Esaki N., Yoshizawa K.;
RT "The catalytic mechanism of fluoroacetate dehalogenase: a computational
RT exploration of biological dehalogenation.";
RL Chemistry 15:7394-7403(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, ACTIVE
RP SITE, FUNCTION, MUTAGENESIS OF PHE-34; ASP-104; ARG-105; ARG-108; ASP-128;
RP TYR-147; HIS-149; TRP-150; TRP-179; TYR-212; HIS-271 AND PHE-272, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FA1;
RX PubMed=19218394; DOI=10.1128/jb.01654-08;
RA Jitsumori K., Omi R., Kurihara T., Kurata A., Mihara H., Miyahara I.,
RA Hirotsu K., Esaki N.;
RT "X-Ray crystallographic and mutational studies of fluoroacetate
RT dehalogenase from Burkholderia sp. strain FA1.";
RL J. Bacteriol. 191:2630-2637(2009).
CC -!- FUNCTION: Catalyzes the hydrolytic defluorination of fluoroacetate to
CC produce glycolate. Has only very low activity towards chloroacetate.
CC {ECO:0000269|PubMed:19218394, ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a haloacetate + H2O = a halide anion + glycolate + H(+);
CC Xref=Rhea:RHEA:11044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:29805, ChEBI:CHEBI:85638; EC=3.8.1.3;
CC Evidence={ECO:0000269|PubMed:19218394, ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.1 mM for fluoroacetate {ECO:0000269|PubMed:19218394,
CC ECO:0000269|Ref.1};
CC Vmax=61 umol/min/mg enzyme {ECO:0000269|PubMed:19218394,
CC ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:19218394,
CC ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19218394, ECO:0000269|Ref.1}.
CC -!- INDUCTION: Up-regulated by fluoroacetate. Not detectable in the absence
CC of fluoroacetate, or when cells are grown on Luria broth.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB259121; BAE94252.1; -; Genomic_DNA.
DR PDB; 1Y37; X-ray; 1.50 A; A/B=1-304.
DR PDB; 3B12; X-ray; 1.20 A; A/B=1-304.
DR PDBsum; 1Y37; -.
DR PDBsum; 3B12; -.
DR AlphaFoldDB; Q1JU72; -.
DR SMR; Q1JU72; -.
DR ESTHER; bursp-deha; Haloacetate_dehalogenase.
DR BRENDA; 3.8.1.3; 1033.
DR EvolutionaryTrace; Q1JU72; -.
DR GO; GO:0018785; F:haloacetate dehalogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase.
FT CHAIN 1..304
FT /note="Fluoroacetate dehalogenase"
FT /id="PRO_0000398585"
FT DOMAIN 26..151
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 104
FT /note="Nucleophile"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149..150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Important for enzyme activity"
FT MUTAGEN 34
FT /note="F->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 104
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 105
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 108
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 128
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 147
FT /note="Y->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 149
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 150
FT /note="W->A,F,K,Q,R,Y: Abolishes fluoroacetate dehalogenase
FT activity, but does not abolish activity towards
FT chloroacetate."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 179
FT /note="W->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 212
FT /note="Y->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 271
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT MUTAGEN 272
FT /note="F->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19218394"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 13..23
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:3B12"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:3B12"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:3B12"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3B12"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3B12"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:3B12"
SQ SEQUENCE 304 AA; 34087 MW; 0EE1B70133C7F8F2 CRC64;
MFEGFERRLV DVGDVTINCV VGGSGPALLL LHGFPQNLHM WARVAPLLAN EYTVVCADLR
GYGGSSKPVG APDHANYSFR AMASDQRELM RTLGFERFHL VGHDRGGRTG HRMALDHPDS
VLSLAVLDII PTYVMFEEVD RFVARAYWHW YFLQQPAPYP EKVIGADPDT FYEGCLFGWG
ATGADGFDPE QLEEYRKQWR DPAAIHGSCC DYRAGGTIDF ELDHGDLGRQ VQCPALVFSG
SAGLMHSLFE MQVVWAPRLA NMRFASLPGG HFFVDRFPDD TARILREFLS DARSGIHQTE
RRES
