ID   A3LU64_PICST            Unreviewed;       255 AA.
AC   A3LU64;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   02-SEP-2026, entry version 84.
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   Name=GLO2 {ECO:0000313|EMBL:ABN66189.2};
GN   ORFNames=PICST_31656 {ECO:0000313|EMBL:ABN66189.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66189.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN66189.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000498; ABN66189.2; -; Genomic_DNA.
DR   RefSeq; XP_001384218.2; XM_001384181.1.
DR   AlphaFoldDB; A3LU64; -.
DR   FunCoup; A3LU64; 518.
DR   STRING; 322104.A3LU64; -.
DR   GeneID; 4838852; -.
DR   KEGG; pic:PICST_31656; -.
DR   eggNOG; KOG0813; Eukaryota.
DR   HOGENOM; CLU_030571_4_0_1; -.
DR   InParanoid; A3LU64; -.
DR   OMA; NYIWLLQ; -.
DR   OrthoDB; 515692at2759; -.
DR   UniPathway; UPA00619; UER00676.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051596; P:methylglyoxal catabolic process; 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   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   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABN66189.2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          14..177
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   255 AA;  28725 MW;  6DD81E6C6C080C78 CRC64;
     MHIESIPMRW GTGDNYAYLL VDTPTKHAWL IDPAEPDEVV KYFAQNGTQF ELKAIVNTHH
     HYDHAGGNND FHRKYPDLPV IAGKDSPVVS YTPSHQEVID LGDNLSITAL HTPCHTQDSI
     CYYVEDTSTG DRAVFTGDTL FISGCGRFFE GTGEEMDKAL NHVLGSLPKN TRVYPGHEYT
     RSNVKFSKTV IENEAIKKLE AFAKENEYTT GKFTIGDELE FNPFMRLADP VVQKKTGFAK
     PAEVMTKLRE MKNSF
//