DEH1_MORSB
ID DEH1_MORSB Reviewed; 294 AA.
AC Q01398;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Haloacetate dehalogenase H-1;
DE EC=3.8.1.3;
GN Name=dehH1;
OS Moraxella sp. (strain B).
OG Plasmid POU1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella; unclassified Moraxella.
OX NCBI_TaxID=118147;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX PubMed=1512562; DOI=10.1099/00221287-138-7-1317;
RA Kawasaki H., Tsuda K., Matsushita I., Tonomura K.;
RT "Lack of homology between two haloacetate dehalogenase genes encoded on a
RT plasmid from Moraxella sp. strain B.";
RL J. Gen. Microbiol. 138:1317-1323(1992).
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 -!- MISCELLANEOUS: Two haloacetate dehalogenase enzymes exist in Moraxella
CC strain B. DehH1 acts predominantly on fluoroacetate, dehH2 acts on
CC chloro-, bromo- and iodoacetate, but not on fluoroacetate.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
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DR EMBL; D90422; BAA14412.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01398; -.
DR SMR; Q01398; -.
DR ESTHER; morsp-deh1; Haloacetate_dehalogenase.
DR KEGG; ag:BAA14412; -.
DR BioCyc; MetaCyc:MON-15937; -.
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 Direct protein sequencing; Hydrolase; Plasmid.
FT CHAIN 1..294
FT /note="Haloacetate dehalogenase H-1"
FT /id="PRO_0000207070"
FT DOMAIN 27..277
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 33308 MW; 7BA7F07359182703 CRC64;
MDFPGFKNST VTVDGVDIAY TVSGEGPPVL MLHGFPQNRA MWARVAPQLA EHHTVVCADL
RGYGDSDKPK CLPDRSNYSF RTFAHDQLCV MRHLGFERFH LVGHDRGGRT GHRMALDHPE
AVLSLTVMDI VPTYAMFMNT NRLVAASYWH WYFLQQPEPF PEHMIGQDPD FFYETCLFGW
GATKVSDFDQ QMLNAYRESW RNPAMIHGSC SDYRAAATID LEHDSADIQR KVECPTLVFY
GSKGQMGQLF DIPAEWAKRC NNTTNASLPG GHFFVDQFPA ETSEILLKFL ARNG