ID G7JJ86_MEDTR Unreviewed; 281 AA.
AC G7JJ86;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081};
DE AltName: Full=Glyoxalase I {ECO:0000256|ARBA:ARBA00030537};
GN Name=11439567 {ECO:0000313|EnsemblPlants:AES92643};
GN OrderedLocusNames=MTR_4g132260 {ECO:0000313|EMBL:AES92643.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES92643.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES92643.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES92643.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES92643,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AES92643.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES92643,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:AES92643}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES92643};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC {ECO:0000256|ARBA:ARBA00010363}.
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DR EMBL; CM001220; AES92643.1; -; Genomic_DNA.
DR RefSeq; XP_003610446.1; XM_003610398.1.
DR AlphaFoldDB; G7JJ86; -.
DR SMR; G7JJ86; -.
DR STRING; 3880.G7JJ86; -.
DR PaxDb; 3880-AES92642; -.
DR EnsemblPlants; AES92643; AES92643; MTR_4g132260.
DR GeneID; 11439567; -.
DR Gramene; AES92643; AES92643; MTR_4g132260.
DR KEGG; mtr:11439567; -.
DR eggNOG; KOG2943; Eukaryota.
DR HOGENOM; CLU_030607_2_0_1; -.
DR OrthoDB; 2076575at2759; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000002051; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:SF8; 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; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AES92643.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 15..139
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 145..273
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 69
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 87
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 281 AA; 31468 MW; 5138AD952A1C3A2D CRC64;
MAEIDLEWPK KDNRRLLHVV YRVGDLERTI KFYTEALGMK LLRQRDVPEE KYANAFVGFG
DEHSHFAVEL TYNYGVTSYD VGDGFGHFAI ATQDVYKLVE HIRAKGGNIT REAGPVQGGT
TVIAFVKDPD GYTFALVQRP IVHDPFCQIS LRVGDLERAI KFYEKALGLK VVRKVDNPEN
KYTIAILGYK EEDDATVLEL TYNYGVTEYS KGTAYAQIAI GTDDVYKSAD VVNLVTQELG
GEITLQPGPI PGLNTKVTSF LDPDGWKTAL VDNEDFLKEL E
//
