LGUL_SCHPO
ID LGUL_SCHPO Reviewed; 302 AA.
AC Q09751;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5 {ECO:0000269|PubMed:15042280};
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=glo1; ORFNames=SPBC12C2.12c, SPBC21D10.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RX PubMed=15042280; DOI=10.1007/s00203-004-0666-4;
RA Takatsume Y., Izawa S., Inoue Y.;
RT "Identification of thermostable glyoxalase I in the fission yeast
RT Schizosaccharomyces pombe.";
RL Arch. Microbiol. 181:371-377(2004).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione.
CC {ECO:0000269|PubMed:15042280}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5;
CC Evidence={ECO:0000269|PubMed:11859360};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19071;
CC Evidence={ECO:0000305|PubMed:15042280};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15042280};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:15042280};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:15042280};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15042280};
CC Note=Binds 1 zinc ion per subunit. Cobalt, nickel and manganese ions
CC can also function as cofactors. {ECO:0000269|PubMed:15042280};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for methylglyoxal (at pH 7.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15042280};
CC KM=0.8 mM for glutathione (at pH 7.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15042280};
CC KM=0.24 mM for phenylglyoxal (at pH 7.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15042280};
CC Vmax=2 mmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.0
CC and 25 degrees Celsius) {ECO:0000269|PubMed:15042280};
CC Vmax=197 umol/min/mg enzyme with phenylglyoxal as substrate (at pH
CC 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:15042280};
CC pH dependence:
CC Optimum pH is 5.5-7.5. {ECO:0000269|PubMed:15042280};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000305|PubMed:15042280}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15042280}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20759.1; -; Genomic_DNA.
DR PIR; T11675; T11675.
DR RefSeq; NP_596010.1; NM_001021918.2.
DR AlphaFoldDB; Q09751; -.
DR SMR; Q09751; -.
DR BioGRID; 276288; 22.
DR STRING; 4896.SPBC12C2.12c.1; -.
DR MaxQB; Q09751; -.
DR PaxDb; Q09751; -.
DR EnsemblFungi; SPBC12C2.12c.1; SPBC12C2.12c.1:pep; SPBC12C2.12c.
DR GeneID; 2539736; -.
DR KEGG; spo:SPBC12C2.12c; -.
DR PomBase; SPBC12C2.12c; glo1.
DR VEuPathDB; FungiDB:SPBC12C2.12c; -.
DR eggNOG; KOG2944; Eukaryota.
DR HOGENOM; CLU_046006_0_1_1; -.
DR InParanoid; Q09751; -.
DR OMA; MGDAWGH; -.
DR PhylomeDB; Q09751; -.
DR Reactome; R-SPO-70268; Pyruvate metabolism.
DR SABIO-RK; Q09751; -.
DR UniPathway; UPA00619; UER00675.
DR PRO; PR:Q09751; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR GO; GO:0071470; P:cellular response to osmotic stress; TAS:PomBase.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:PomBase.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IMP:PomBase.
DR Gene3D; 3.10.180.10; -; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; SSF54593; 2.
DR TIGRFAMs; TIGR00068; glyox_I; 2.
DR PROSITE; PS00934; GLYOXALASE_I_1; 2.
DR PROSITE; PS00935; GLYOXALASE_I_2; 2.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Cobalt; Lyase; Manganese; Metal-binding; Nickel; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..302
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000168086"
FT DOMAIN 11..153
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 166..301
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 302 AA; 34410 MW; D5F916F51BA2A0F5 CRC64;
MASTTDMSTY KLNHTMIRVK DLDKSLKFYT EVFGMKLIDQ WVFEENEFSL SFLAFDGPGA
LNHGVERSKR EGILELTYNF GTEKKEGPVY INGNTEPKRG FGHICFTVDN IESACAYLES
KGVSFKKKLS DGKMKHIAFA LDPDNYWIEL VSQSETKPKA NISNFRFNHT MVRVKDPEPS
IAFYEKLGMK VIDKADHPNG KFTNYFLAYP SDLPRHDREG LLELTHNWGT EKESGPVYHN
GNDGDEKGYG HVCISVDNIN AACSKFEAEG LPFKKKLTDG RMKDIAFLLD PDNYWVEVIE
QK
