GLX1_ARATH
ID GLX1_ARATH Reviewed; 283 AA.
AC O65398; B9DFN6; B9DGT0; F4IAH9; Q3EDE2; Q940A4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Lactoylglutathione lyase GLX1 {ECO:0000303|PubMed:17404219};
DE EC=4.4.1.5 {ECO:0000250|UniProtKB:Q04760};
DE AltName: Full=Glyoxalase I {ECO:0000303|PubMed:17404219};
DE Short=AtGLX1 {ECO:0000303|PubMed:17404219};
DE Short=GlyI {ECO:0000303|PubMed:17404219};
GN Name=GLX1 {ECO:0000303|PubMed:17404219};
GN OrderedLocusNames=At1g11840 {ECO:0000312|Araport:AT1G11840};
GN ORFNames=F12F1.32 {ECO:0000312|EMBL:AAC17630.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=cv. Columbia; TISSUE=Root, and Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION BY SNRK2.8.
RX PubMed=17404219; DOI=10.1073/pnas.0610208104;
RA Shin R., Alvarez S., Burch A.Y., Jez J.M., Schachtman D.P.;
RT "Phosphoproteomic identification of targets of the Arabidopsis sucrose
RT nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic
RT processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6460-6465(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione.
CC {ECO:0000250|UniProtKB:Q04760}.
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:0000250|UniProtKB:Q04760};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9CPU0};
CC Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are
CC bound between subunits. {ECO:0000250|UniProtKB:Q9CPU0};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000250|UniProtKB:Q04760}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q04760}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O65398-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O65398-2; Sequence=VSP_059032;
CC Name=3;
CC IsoId=O65398-3; Sequence=VSP_059033, VSP_059034;
CC -!- PTM: Phosphorylated by SnRK2.8. {ECO:0000269|PubMed:17404219}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; AC002131; AAC17630.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28792.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28793.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28794.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28795.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28796.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28797.1; -; Genomic_DNA.
DR EMBL; AB050553; BAB17665.1; -; mRNA.
DR EMBL; AF428272; AAL16104.1; -; mRNA.
DR EMBL; AY056148; AAL07227.1; -; mRNA.
DR EMBL; AY074569; AAL67109.1; -; mRNA.
DR EMBL; AY097360; AAM19876.1; -; mRNA.
DR EMBL; AK316841; BAH19553.1; -; mRNA.
DR EMBL; AK317270; BAH19947.1; -; mRNA.
DR EMBL; AK318730; BAH56845.1; -; mRNA.
DR EMBL; AY087874; AAM65426.1; -; mRNA.
DR PIR; F86252; F86252.
DR RefSeq; NP_001031025.1; NM_001035948.1. [O65398-1]
DR RefSeq; NP_001031026.1; NM_001035949.3. [O65398-3]
DR RefSeq; NP_001184968.1; NM_001198039.1. [O65398-2]
DR RefSeq; NP_172648.1; NM_101055.4. [O65398-1]
DR RefSeq; NP_849643.1; NM_179312.4. [O65398-1]
DR RefSeq; NP_849644.2; NM_179313.2. [O65398-1]
DR AlphaFoldDB; O65398; -.
DR SMR; O65398; -.
DR IntAct; O65398; 2.
DR STRING; 3702.AT1G11840.6; -.
DR iPTMnet; O65398; -.
DR SwissPalm; O65398; -.
DR PRIDE; O65398; -.
DR ProMEX; O65398; -.
DR ProteomicsDB; 247404; -. [O65398-1]
DR EnsemblPlants; AT1G11840.1; AT1G11840.1; AT1G11840. [O65398-1]
DR EnsemblPlants; AT1G11840.2; AT1G11840.2; AT1G11840. [O65398-1]
DR EnsemblPlants; AT1G11840.3; AT1G11840.3; AT1G11840. [O65398-1]
DR EnsemblPlants; AT1G11840.4; AT1G11840.4; AT1G11840. [O65398-1]
DR EnsemblPlants; AT1G11840.5; AT1G11840.5; AT1G11840. [O65398-3]
DR EnsemblPlants; AT1G11840.6; AT1G11840.6; AT1G11840. [O65398-2]
DR GeneID; 837731; -.
DR Gramene; AT1G11840.1; AT1G11840.1; AT1G11840. [O65398-1]
DR Gramene; AT1G11840.2; AT1G11840.2; AT1G11840. [O65398-1]
DR Gramene; AT1G11840.3; AT1G11840.3; AT1G11840. [O65398-1]
DR Gramene; AT1G11840.4; AT1G11840.4; AT1G11840. [O65398-1]
DR Gramene; AT1G11840.5; AT1G11840.5; AT1G11840. [O65398-3]
DR Gramene; AT1G11840.6; AT1G11840.6; AT1G11840. [O65398-2]
DR KEGG; ath:AT1G11840; -.
DR Araport; AT1G11840; -.
DR TAIR; locus:2008930; AT1G11840.
DR eggNOG; KOG2943; Eukaryota.
DR HOGENOM; CLU_030607_2_0_1; -.
DR OMA; MGDAWGH; -.
DR OrthoDB; 1513831at2759; -.
DR PhylomeDB; O65398; -.
DR BioCyc; ARA:AT1G11840-MON; -.
DR UniPathway; UPA00619; UER00675.
DR PRO; PR:O65398; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65398; baseline and differential.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:TAIR.
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; IGI:TAIR.
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; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Dioxygenase; Lyase; Manganese;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..283
FT /note="Lactoylglutathione lyase GLX1"
FT /id="PRO_0000441174"
FT DOMAIN 17..141
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 147..275
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 20
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 24
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 71
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 75
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 89
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 137
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 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 150
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9CPU0"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9CPU0"
FT BINDING 154
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9CPU0"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9CPU0"
FT BINDING 205
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9CPU0"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 251..252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9CPU0"
FT BINDING 271
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1
FT /note="M -> MNEIASASMLRLCQCFISICNVHFVSMRAAESSFLLSRNM (in
FT isoform 2)"
FT /id="VSP_059032"
FT VAR_SEQ 220..232
FT /note="IAIGTDDVYKSGE -> AQMMCTKAVKLLR (in isoform 3)"
FT /id="VSP_059033"
FT VAR_SEQ 233..283
FT /note="Missing (in isoform 3)"
FT /id="VSP_059034"
FT CONFLICT 40
FT /note="G -> C (in Ref. 5; BAH19947)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="R -> W (in Ref. 4; AAL07227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 31928 MW; A321FECFCD2EAFE9 CRC64;
MAEASDLLEW PKKDNRRFLH VVYRVGDLDR TIEFYTEVFG MKLLRKRDIP EEKYSNAFLG
FGPETSNFVV ELTYNYGVSS YDIGTGFGHF AISTQDVSKL VENVRAKGGN VTREPGPVKG
GGSVIAFVKD PDGYTFELIQ RGPTPEPFCQ VMLRVGDLDR AIKFYEKALG MRLLRKIERP
EYKYTIGMMG YAEEYESIVL ELTYNYDVTE YTKGNAYAQI AIGTDDVYKS GEVIKIVNQE
LGGKITREAG PLPGLGTKIV SFLDPDGWKT VLVDNKDFLK ELE
