GLO2M_ARATH
ID GLO2M_ARATH Reviewed; 331 AA.
AC O24495; O22857; O24494;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Hydroxyacylglutathione hydrolase 1, mitochondrial;
DE EC=3.1.2.6;
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
DE Flags: Precursor;
GN Name=GLX2-1; Synonyms=GLY1; OrderedLocusNames=At2g43430; ORFNames=T1O24.17;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9349270; DOI=10.1023/a:1005891123344;
RA Maiti M.K., Krishnasamy S., Owen H.A., Makaroff C.A.;
RT "Molecular characterization of glyoxalase II from Arabidopsis thaliana.";
RL Plant Mol. Biol. 35:471-481(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O24496};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:O24496};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O24496};
CC Note=Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit. Electron
CC spin resonance indicates the presence of a mixture of protein molecules
CC that contain either Fe(2+) or Zn(2+). {ECO:0000250|UniProtKB:O24496};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
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=O24495-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots, flowers and flower buds.
CC Also detected in leaves. {ECO:0000269|PubMed:9349270}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; U90927; AAC49865.1; -; Genomic_DNA.
DR EMBL; U90928; AAC49866.1; -; mRNA.
DR EMBL; AC002335; AAB64315.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10268.1; -; Genomic_DNA.
DR EMBL; AY091278; AAM14217.1; -; mRNA.
DR EMBL; AY063806; AAL36162.1; -; mRNA.
DR PIR; A84866; A84866.
DR RefSeq; NP_565999.1; NM_129904.3. [O24495-1]
DR AlphaFoldDB; O24495; -.
DR SMR; O24495; -.
DR STRING; 3702.AT2G43430.1; -.
DR PaxDb; O24495; -.
DR PRIDE; O24495; -.
DR ProteomicsDB; 248585; -. [O24495-1]
DR EnsemblPlants; AT2G43430.1; AT2G43430.1; AT2G43430. [O24495-1]
DR GeneID; 818944; -.
DR Gramene; AT2G43430.1; AT2G43430.1; AT2G43430. [O24495-1]
DR KEGG; ath:AT2G43430; -.
DR Araport; AT2G43430; -.
DR TAIR; locus:2058239; AT2G43430.
DR eggNOG; KOG0813; Eukaryota.
DR InParanoid; O24495; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; O24495; -.
DR UniPathway; UPA00619; UER00676.
DR PRO; PR:O24495; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O24495; baseline and differential.
DR Genevisible; O24495; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:TAIR.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR GO; GO:0043200; P:response to amino acid; IMP:TAIR.
DR GO; GO:0034059; P:response to anoxia; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR001018; Beta-lactamase_class-B_CS.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Iron; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..76
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 77..331
FT /note="Hydroxyacylglutathione hydrolase 1, mitochondrial"
FT /id="PRO_0000012286"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 246..248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT CONFLICT 159
FT /note="D -> H (in Ref. 1; AAC49866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36500 MW; 2EDC21B4902419C5 CRC64;
MPVISKASST TTNSSIPSCS RIGGQLCVWP GLRQLCLRKS LLYGVMWLLS MPLKTLRGAR
KTLKITHFCS ISNMPSSLKI ELVPCSKDNY AYLLHDEDTG TVGVVDPSEA APVIEALSRK
NWNLTYILNT HHHDDHIGGN AELKERYGAK VIGSAVDKDR IPGIDILLKD SDKWMFAGHE
VRILDTPGHT QGHISFYFPG SATIFTGDLI YSLSCGTLSE GTPEQMLSSL QKIVSLPDDT
NIYCGRENTA GNLKFALSVE PKNETLQSYA TRVAHLRSQG LPSIPTTVKV EKACNPFLRI
SSKDIRKSLS IPDSATEAEA LRRIQRARDR F
