LGUC_ARATH
ID LGUC_ARATH Reviewed; 350 AA.
AC Q8W593; A8MRZ1; Q8LEY7; Q9FYG5;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable lactoylglutathione lyase, chloroplastic;
DE EC=4.4.1.5;
DE AltName: Full=Glyoxalase I;
DE Flags: Precursor;
GN OrderedLocusNames=At1g67280; ORFNames=F1N21.10;
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=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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 62-71, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11719511}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W593-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W593-2; Sequence=VSP_038976;
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00253.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002130; AAG00253.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34621.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34622.1; -; Genomic_DNA.
DR EMBL; AF419551; AAL31884.1; -; mRNA.
DR EMBL; AY079102; AAL84986.1; -; mRNA.
DR EMBL; AY085148; AAM61701.1; -; mRNA.
DR PIR; E96696; E96696.
DR RefSeq; NP_001077783.1; NM_001084314.2. [Q8W593-2]
DR RefSeq; NP_176896.1; NM_105396.4. [Q8W593-1]
DR AlphaFoldDB; Q8W593; -.
DR SMR; Q8W593; -.
DR BioGRID; 28269; 1.
DR STRING; 3702.AT1G67280.1; -.
DR MetOSite; Q8W593; -.
DR PaxDb; Q8W593; -.
DR PRIDE; Q8W593; -.
DR ProteomicsDB; 238435; -. [Q8W593-1]
DR EnsemblPlants; AT1G67280.1; AT1G67280.1; AT1G67280. [Q8W593-1]
DR EnsemblPlants; AT1G67280.2; AT1G67280.2; AT1G67280. [Q8W593-2]
DR GeneID; 843048; -.
DR Gramene; AT1G67280.1; AT1G67280.1; AT1G67280. [Q8W593-1]
DR Gramene; AT1G67280.2; AT1G67280.2; AT1G67280. [Q8W593-2]
DR KEGG; ath:AT1G67280; -.
DR Araport; AT1G67280; -.
DR TAIR; locus:2019574; AT1G67280.
DR eggNOG; KOG2943; Eukaryota.
DR HOGENOM; CLU_030607_0_0_1; -.
DR InParanoid; Q8W593; -.
DR OMA; GCEAACN; -.
DR PhylomeDB; Q8W593; -.
DR BioCyc; ARA:AT1G67280-MON; -.
DR UniPathway; UPA00619; UER00675.
DR PRO; PR:Q8W593; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W593; baseline and differential.
DR Genevisible; Q8W593; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
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 GO; GO:0009409; P:response to cold; IEP: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; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing; Lyase;
KW Metal-binding; Plastid; Reference proteome; Repeat; Transit peptide; Zinc.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 62..350
FT /note="Probable lactoylglutathione lyase, chloroplastic"
FT /id="PRO_0000393414"
FT DOMAIN 88..212
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 218..342
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 208
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038976"
FT CONFLICT 72
FT /note="A -> S (in Ref. 4; AAM61701)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> S (in Ref. 4; AAM61701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39167 MW; E02C0AA2483E0424 CRC64;
MVRIIPMAAS SIRPSLACFS DSPRFPISLL SRNLSRTLHV PQSQLFGLTS HKLLRRSVNC
LGVAESGKAA QATTQDDLLT WVKNDKRRML HVVYRVGDMD RTIKFYTECL GMKLLRKRDI
PEEKYTNAFL GYGPEDSHFV IELTYNYGVD KYDIGAGFGH FGIAVDDVAK TVELVKAKGG
KVSREPGPVK GGKTVIAFIE DPDGYKFELL ERGPTPEPLC QVMLRVGDLD RAIKFYEKAF
GMELLRTRDN PEYKYTIAMM GYGPEDKFPV LELTYNYGVT EYDKGNAYAQ IAIGTDDVYK
TAEAIKLFGG KITREPGPLP GISTKITACL DPDGWKSVFV DNIDFLKELE
