GLO2_SCHMA
ID GLO2_SCHMA Reviewed; 240 AA.
AC Q26547;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable hydroxyacylglutathione hydrolase;
DE EC=3.1.2.6;
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=7665603; DOI=10.1074/jbc.270.37.21813;
RA Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.;
RT "RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes
RT in the human parasite, Schistosoma mansoni.";
RL J. Biol. Chem. 270:21813-21819(1995).
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q16775};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; U30264; AAC46899.1; -; mRNA.
DR STRING; 6183.Smp_091010.1; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_030571_4_0_1; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
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; -; 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 Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..240
FT /note="Probable hydroxyacylglutathione hydrolase"
FT /id="PRO_0000192345"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 234..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
SQ SEQUENCE 240 AA; 26590 MW; 0E910F5CB48A59D9 CRC64;
MSSEQLQDPV EPDKILSAVT QRGLRLESIL TTHHHLDHAG GNLDLVTKCR KQGLEGLKVY
GGDDRIGGLT DTVSHGYKXR LVATSTFIAW LHHRHTTGHI CYLVTEENST KEGAVFTGDT
LFLGGCGRFF EGTAEQMFKA LIEVLSKLPT TTKVYCGHEY TVKNLEFGLT VEPKNEALKH
RLEAVKRLRA SNQASVPGTI GEELATNPLM RVSEPDVLAH AKTTDPIKAM KTIREEKDRF
