ID A0A3R7J2X4_9STRA Unreviewed; 260 AA.
AC A0A3R7J2X4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=hydroxyacylglutathione hydrolase {ECO:0000256|ARBA:ARBA00011917};
DE EC=3.1.2.6 {ECO:0000256|ARBA:ARBA00011917};
DE AltName: Full=Glyoxalase II {ECO:0000256|ARBA:ARBA00031044};
GN ORFNames=BBI17_008893 {ECO:0000313|EMBL:RLN44689.1}, BBO99_00008878
GN {ECO:0000313|EMBL:RLN74557.1}, JM16_008629
GN {ECO:0000313|EMBL:KAG2509809.1}, JM18_008745
GN {ECO:0000313|EMBL:KAG2510963.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN74557.1, ECO:0000313|Proteomes:UP000285624};
RN [1] {ECO:0000313|EMBL:KAG2509809.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2509809.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2510963.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN44689.1}, and Chile4
RC {ECO:0000313|EMBL:RLN74557.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2509809.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2509809.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2510963.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
CC {ECO:0000256|ARBA:ARBA00004015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001623};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004963}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN74557.1}.
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; JPWV03000517; KAG2509809.1; -; Genomic_DNA.
DR EMBL; JPWU03000555; KAG2510963.1; -; Genomic_DNA.
DR EMBL; MAYM02000266; RLN44689.1; -; Genomic_DNA.
DR EMBL; MBDN02000542; RLN74557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7J2X4; -.
DR STRING; 325452.A0A3R7J2X4; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; Unassembled WGS sequence.
DR Proteomes; UP000792063; Unassembled WGS sequence.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR NCBIfam; TIGR03413; GSH_gloB; 1.
DR PANTHER; PTHR11935; BETA LACTAMASE DOMAIN; 1.
DR PANTHER; PTHR11935:SF94; TENZING NORGAY, ISOFORM C; 1.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 13..174
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 260 AA; 28649 MW; 97B1EAB6B6F25F11 CRC64;
MTMQIELIPV LSDNYAYLLI DPTNRVAAAV DPVDAEKVHA RAQELKLKIE MILTTHSHWD
HAGGNRDLSE LILQRDGRDI PVIGGPGAAV EAATRSVSEG ETIALGELQI KVYFTPCHTR
DHVLYHCQDA LFTGDTLFVA GCGRFFSGSP AEMHHALNEV VAKLPEGTKI YCGHEYTSSN
LRFAAYVEPD NAVIQEKLVW AIKKTEEGEP TIPSTVKEEL ETNPFMRVNH ADVQKFAKEK
DPVAVMGAVR AAKDNFVIGK
//
