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Database: UniProt
Entry: A0A2T7CD27_9POAL
LinkDB: A0A2T7CD27_9POAL
Original site: A0A2T7CD27_9POAL 
ID   A0A2T7CD27_9POAL        Unreviewed;       258 AA.
AC   A0A2T7CD27;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=GQ55_9G488200 {ECO:0000313|EMBL:PUZ41239.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ41239.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ41239.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) 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}.
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DR   EMBL; CM009757; PUZ41239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7CD27; -.
DR   STRING; 1504633.A0A2T7CD27; -.
DR   EnsemblPlants; PUZ41239; PUZ41239; GQ55_9G488200.
DR   Gramene; PUZ41239; PUZ41239; GQ55_9G488200.
DR   Proteomes; UP000244336; Chromosome 9.
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:UP000244336};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          11..174
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   258 AA;  28633 MW;  9689FAFE2FB163D5 CRC64;
     MKIIPVPCLE DNYAYLIVDE STKKAAAVDP VEPEKVLKAA SEVGASVDCV LTTHHHWDHA
     GGNEKMKLQV PGIKVFGGSL DNVKGCTDQV ENGTKLSLGK DIEILCLHTP CHTKGHISYY
     VTSKEGEDPA VFTGDTLFIA GCGRFFEGTA EQMYQSLIVT LGSLPKSTRV YCGHEYTVKS
     LKFMLTLEPE NEKTKQKLEW AEKQREANQP TVPSTIGDEF EINTFMRVDL PEIQAKFSAK
     SPVEALREVR KIKDNWKG
//
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