ID I1PTJ0_ORYGL Unreviewed; 350 AA.
AC I1PTJ0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081, ECO:0000256|RuleBase:RU361179};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081, ECO:0000256|RuleBase:RU361179};
DE AltName: Full=Glyoxalase I {ECO:0000256|ARBA:ARBA00030537, ECO:0000256|RuleBase:RU361179};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA05G0068800.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA05G0068800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione.
CC {ECO:0000256|RuleBase:RU361179}.
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:0000256|ARBA:ARBA00000817,
CC ECO:0000256|RuleBase:RU361179};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR604361-3};
CC Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are
CC bound between subunits. {ECO:0000256|PIRSR:PIRSR604361-3};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005008, ECO:0000256|RuleBase:RU361179}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC {ECO:0000256|ARBA:ARBA00010363, ECO:0000256|RuleBase:RU361179}.
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DR AlphaFoldDB; I1PTJ0; -.
DR STRING; 4538.I1PTJ0; -.
DR EnsemblPlants; ORGLA05G0068800.1; ORGLA05G0068800.1; ORGLA05G0068800.
DR Gramene; ORGLA05G0068800.1; ORGLA05G0068800.1; ORGLA05G0068800.
DR eggNOG; KOG2943; Eukaryota.
DR HOGENOM; CLU_030607_2_0_1; -.
DR OMA; GCEAACN; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd16358; GlxI_Ni; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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 NCBIfam; TIGR00068; glyox_I; 1.
DR PANTHER; PTHR46036; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR46036:SF5; LACTOYLGLUTATHIONE LYASE; 1.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR PROSITE; PS00934; GLYOXALASE_I_1; 2.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
DR PROSITE; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361179};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3,
KW ECO:0000256|RuleBase:RU361179}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3, ECO:0000256|RuleBase:RU361179}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..350
FT /note="Lactoylglutathione lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012836238"
FT DOMAIN 87..211
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 217..341
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 207
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
SQ SEQUENCE 350 AA; 38540 MW; 9D7F5E55316C4C32 CRC64;
MARLLLPLPI AAAAASRLRL PVLSSSVARR EALLFGGRVA AARAPVRLAR RGVSAGAEAG
GSSSAAAAAQ VIGQDEAVEW VKKDRRRMLH VVYRVGDLDK TIKFYTECLG MKLLRKRDIP
EERYTNAFLG YGPEDSHFVV ELTYNYGVES YDIGTAFGHF GIAVEDVAKT VDLIKAKGGT
VTREPGPVKG GKSVIAFIED PDGYKFELIE RGPTPEPLCQ VMLRVGDLDR AINFYEKAFG
MELLRKRDNP QYKYTIAMMG YGPEDKNAVL ELTYNYGVKE YDKGNAYAQI AISTDDVYKT
AEVIRQNGGQ ITREPGPLPG INTKITACTD PDGWKTVFVD NVDFLKELEE
//
