LGUL_ARATH
ID LGUL_ARATH Reviewed; 185 AA.
AC Q8H0V3; Q9LMZ7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
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 OrderedLocusNames=At1g08110; ORFNames=T6D22.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8H0V3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC026875; AAF79827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28243.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28244.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28245.1; -; Genomic_DNA.
DR EMBL; BT002020; AAN72031.1; -; mRNA.
DR EMBL; BT014867; AAT41850.1; -; mRNA.
DR PIR; G86215; G86215.
DR RefSeq; NP_001030995.1; NM_001035918.2. [Q8H0V3-1]
DR RefSeq; NP_172291.1; NM_100687.4. [Q8H0V3-1]
DR RefSeq; NP_849609.1; NM_179278.2. [Q8H0V3-1]
DR AlphaFoldDB; Q8H0V3; -.
DR SMR; Q8H0V3; -.
DR BioGRID; 22571; 1.
DR STRING; 3702.AT1G08110.4; -.
DR iPTMnet; Q8H0V3; -.
DR MetOSite; Q8H0V3; -.
DR PaxDb; Q8H0V3; -.
DR PRIDE; Q8H0V3; -.
DR ProteomicsDB; 250744; -. [Q8H0V3-1]
DR EnsemblPlants; AT1G08110.1; AT1G08110.1; AT1G08110. [Q8H0V3-1]
DR EnsemblPlants; AT1G08110.2; AT1G08110.2; AT1G08110. [Q8H0V3-1]
DR EnsemblPlants; AT1G08110.3; AT1G08110.3; AT1G08110. [Q8H0V3-1]
DR GeneID; 837330; -.
DR Gramene; AT1G08110.1; AT1G08110.1; AT1G08110. [Q8H0V3-1]
DR Gramene; AT1G08110.2; AT1G08110.2; AT1G08110. [Q8H0V3-1]
DR Gramene; AT1G08110.3; AT1G08110.3; AT1G08110. [Q8H0V3-1]
DR KEGG; ath:AT1G08110; -.
DR Araport; AT1G08110; -.
DR eggNOG; KOG2944; Eukaryota.
DR HOGENOM; CLU_046006_1_3_1; -.
DR InParanoid; Q8H0V3; -.
DR PhylomeDB; Q8H0V3; -.
DR BioCyc; ARA:AT1G08110-MON; -.
DR UniPathway; UPA00619; UER00675.
DR PRO; PR:Q8H0V3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H0V3; baseline and differential.
DR Genevisible; Q8H0V3; AT.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR Gene3D; 3.10.180.10; -; 1.
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; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
DR PROSITE; PS51819; VOC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..185
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000168080"
FT DOMAIN 27..174
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 185 AA; 20848 MW; 93ED7F1E9E8353FA CRC64;
MASEARESPA NNPGLSTNRD EATKGYIMQQ TMFRIKDPKA SLDFYSRVLG MSLLKRLDFS
EMKFSLYFLG YEDTTTAPTD PTERTVWTFG QPATIELTHN WGTESDPEFK GYHNGNSEPR
GFGHIGVTVD DVHKACERFE ELGVEFAKKP NDGKMKNIAF IKDPDGYWIE IFDLKTIGTT
TVNAA
