GLO2_ENCCU
ID GLO2_ENCCU Reviewed; 249 AA.
AC Q8SSH0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable hydroxyacylglutathione hydrolase ECU02_0580;
DE EC=3.1.2.6;
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
GN OrderedLocusNames=ECU02_0580;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AL590442; CAD25089.2; -; Genomic_DNA.
DR RefSeq; NP_584585.1; NM_001040774.1.
DR AlphaFoldDB; Q8SSH0; -.
DR SMR; Q8SSH0; -.
DR STRING; 284813.Q8SSH0; -.
DR GeneID; 858575; -.
DR KEGG; ecu:ECU02_0580; -.
DR VEuPathDB; MicrosporidiaDB:ECU02_0580; -.
DR HOGENOM; CLU_030571_4_5_1; -.
DR InParanoid; Q8SSH0; -.
DR OrthoDB; 961826at2759; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000000819; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..249
FT /note="Probable hydroxyacylglutathione hydrolase
FT ECU02_0580"
FT /id="PRO_0000383114"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 183..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 240..243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
SQ SEQUENCE 249 AA; 28693 MW; 1BDD732E7E3174B0 CRC64;
MGIEVISILV GGGNNYMHLF YDDDAAFCVD ASNPRILLKA LGINFKKSIY DEKEIFSMGE
DRKKRRELVY LFTTHKHLDH SAGIRCISEE SPNTKTISGF SGDICKSGDK FRFKDVEIEC
FHTPCHTVDS FCFYVGEKYL ATGDTLLFLG CGKFFGGTPG QMIKNIEEIK KRVNHDAVLL
YGHDYSEQNI RFTEEFYHVP EEIKKKKFLK LAEEIKYNPF FNLKKVSIEG SEEEVMGKLR
ERKNKFSKE
