LGUL_ORYSJ
ID LGUL_ORYSJ Reviewed; 291 AA.
AC Q948T6; Q0J7H9; Q9ZWJ2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5 {ECO:0000269|PubMed:11139585};
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Allergen Glb33;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Glyoxylase I 11 {ECO:0000305};
DE Short=OsGLYI-11 {ECO:0000303|PubMed:24661284};
DE Short=OsGLYI11 {ECO:0000303|PubMed:21213008};
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=PP33;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
DE AltName: Allergen=Ory s Glyoxalase I;
GN Name=GLYI-11 {ECO:0000303|PubMed:24661284}; Synonyms=GLX-I;
GN OrderedLocusNames=Os08g0191700, LOC_Os08g09250; ORFNames=OSJNBa0056O06.9-1;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 222-236 AND
RP 267-277, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND ALLERGEN.
RX PubMed=11139585; DOI=10.1074/jbc.m010337200;
RA Usui Y., Nakase M., Hotta H., Urisu A., Aoki N., Kitajima K., Matsuda T.;
RT "A 33-kDa allergen from rice (Oryza sativa L. Japonica). cDNA cloning,
RT expression, and identification as a novel glyoxalase I.";
RL J. Biol. Chem. 276:11376-11381(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of glyoxalase genes in rice seeds.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Structural and expression analysis of germinating seed genes in Oryza
RT sativa L.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP PROTEIN SEQUENCE OF 28-37, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare; TISSUE=Callus, and Panicle;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND PHOSPHORYLATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=16028114; DOI=10.1007/s11103-005-4013-1;
RA Khan M.M.K., Jan A., Karibe H., Komatsu S.;
RT "Identification of phosphoproteins regulated by gibberellin in rice leaf
RT sheath.";
RL Plant Mol. Biol. 58:27-40(2005).
RN [10]
RP INDUCTION.
RX PubMed=21213008; DOI=10.1007/s10142-010-0203-2;
RA Mustafiz A., Singh A.K., Pareek A., Sopory S.K., Singla-Pareek S.L.;
RT "Genome-wide analysis of rice and Arabidopsis identifies two glyoxalase
RT genes that are highly expressed in abiotic stresses.";
RL Funct. Integr. Genomics 11:293-305(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX PubMed=21300107; DOI=10.1016/j.yrtph.2011.01.008;
RA Satoh R., Nakamura R., Komatsu A., Oshima M., Teshima R.;
RT "Proteomic analysis of known and candidate rice allergens between non-
RT transgenic and transgenic plants.";
RL Regul. Toxicol. Pharmacol. 59:437-444(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX PubMed=23763241; DOI=10.1021/pr4002146;
RA Kurokawa S., Nakamura R., Mejima M., Kozuka-Hata H., Kuroda M.,
RA Takeyama N., Oyama M., Satoh S., Kiyono H., Masumura T., Teshima R.,
RA Yuki Y.;
RT "MucoRice-cholera toxin B-subunit, a rice-based oral cholera vaccine, down-
RT regulates the expression of alpha-amylase/trypsin inhibitor-like protein
RT family as major rice allergens.";
RL J. Proteome Res. 12:3372-3382(2013).
RN [13]
RP FUNCTION, ACTIVE SITE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP AND MUTAGENESIS OF GLU-78; GLU-145 AND GLU-209.
RX PubMed=24661284; DOI=10.1111/tpj.12521;
RA Mustafiz A., Ghosh A., Tripathi A.K., Kaur C., Ganguly A.K., Bhavesh N.S.,
RA Tripathi J.K., Pareek A., Sopory S.K., Singla-Pareek S.L.;
RT "A unique Ni2+ -dependent and methylglyoxal-inducible rice glyoxalase I
RT possesses a single active site and functions in abiotic stress response.";
RL Plant J. 78:951-963(2014).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione (By similarity).
CC Involved in the detoxifiation of methylglyoxal. Can functionally
CC complement growth defect of a yeast mutant lacking GLY I. Involved in
CC abiotic stress response. Over-expression of GLYI-11 in tobacco
CC increases tolerance to osmotic, oxidative and salt stresses
CC (PubMed:24661284). {ECO:0000250|UniProtKB:Q04760,
CC ECO:0000269|PubMed:24661284}.
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:11139585};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:24661284};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000269|PubMed:24661284};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for methylglyoxal {ECO:0000269|PubMed:11139585};
CC KM=99.8 uM for glutatione {ECO:0000269|PubMed:24661284};
CC Vmax=130.8 umol/min/mg enzyme with glutatione as substrate
CC {ECO:0000269|PubMed:24661284};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:24661284};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24661284}.
CC -!- TISSUE SPECIFICITY: Expressed in callus, stem, leaves, panicles and
CC maturing seeds (at protein level). {ECO:0000269|PubMed:11139585,
CC ECO:0000269|PubMed:14681440}.
CC -!- INDUCTION: By salt stress and hydrogen peroxide (PubMed:21213008).
CC Induced by methylglyoxal (PubMed:24661284).
CC {ECO:0000269|PubMed:21213008, ECO:0000269|PubMed:24661284}.
CC -!- PTM: Phosphorylated after gibberellin treatment.
CC {ECO:0000269|PubMed:16028114}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:11139585, ECO:0000269|PubMed:21300107,
CC ECO:0000269|PubMed:23763241}.
CC -!- MISCELLANEOUS: Plants over-expressing GLYI-11 display increased
CC tolerance to osmotic, oxidative and salt stresses.
CC {ECO:0000269|PubMed:24661284}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; AB017042; BAA36759.1; -; mRNA.
DR EMBL; EF122487; ABL74574.1; -; mRNA.
DR EMBL; GQ848063; ADM86876.1; -; mRNA.
DR EMBL; AB050986; BAB71741.1; -; Genomic_DNA.
DR EMBL; AP005441; BAD05593.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23086.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT04178.1; -; Genomic_DNA.
DR EMBL; AK066092; BAG89815.1; -; mRNA.
DR EMBL; AK103694; BAG96209.1; -; mRNA.
DR RefSeq; XP_015650705.1; XM_015795219.1.
DR AlphaFoldDB; Q948T6; -.
DR SMR; Q948T6; -.
DR STRING; 4530.OS08T0191700-01; -.
DR Allergome; 1048; Ory s Glyoxalase I.
DR PaxDb; Q948T6; -.
DR PRIDE; Q948T6; -.
DR EnsemblPlants; Os08t0191700-01; Os08t0191700-01; Os08g0191700.
DR EnsemblPlants; Os08t0191700-03; Os08t0191700-03; Os08g0191700.
DR GeneID; 4344858; -.
DR Gramene; Os08t0191700-01; Os08t0191700-01; Os08g0191700.
DR Gramene; Os08t0191700-03; Os08t0191700-03; Os08g0191700.
DR KEGG; osa:4344858; -.
DR eggNOG; KOG2943; Eukaryota.
DR HOGENOM; CLU_030607_2_0_1; -.
DR InParanoid; Q948T6; -.
DR OrthoDB; 1513831at2759; -.
DR BRENDA; 4.4.1.5; 8948.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q948T6; baseline and differential.
DR Genevisible; Q948T6; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:UniProtKB.
DR GO; GO:0016151; F:nickel cation binding; IDA:UniProtKB.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
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; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Lyase; Metal-binding; Nickel;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..291
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000168085"
FT DOMAIN 24..149
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 155..283
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 96
FT /evidence="ECO:0000305|PubMed:24661284"
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:24661284"
FT ACT_SITE 158
FT /evidence="ECO:0000305|PubMed:24661284"
FT ACT_SITE 209
FT /evidence="ECO:0000305|PubMed:24661284"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04760"
FT BINDING 145
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000305|PubMed:24661284"
FT BINDING 209
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000305|PubMed:24661284"
FT MUTAGEN 78
FT /note="E->Q: No effect on the activity."
FT /evidence="ECO:0000269|PubMed:24661284"
FT MUTAGEN 145
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24661284"
FT MUTAGEN 209
FT /note="E->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24661284"
FT CONFLICT 25
FT /note="L -> V (in Ref. 1; BAB71741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32553 MW; 5CB9FEB32F2BC7ED CRC64;
MASGSEAEKS PEVVLEWPKK DKKRLLHAVY RVGDLDRTIK CYTECFGMKL LRKRDVPEEK
YTNAFLGFGP EDTNFALELT YNYGVDKYDI GAGFGHFAIA TEDVYKLAEK IKSSCCCKIT
REPGPVKGGS TVIAFAQDPD GYMFELIQRG PTPEPLCQVM LRVGDLDRSI KFYEKALGMK
LLRKKDVPDY KYTIAMLGYA DEDKTTVIEL TYNYGVTEYT KGNAYAQVAI GTEDVYKSAE
AVELVTKELG GKILRQPGPL PGLNTKIASF LDPDGWKVVL VDNADFLKEL Q
