GLO2C_ARATH
ID GLO2C_ARATH Reviewed; 258 AA.
AC O24496; O04844;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Hydroxyacylglutathione hydrolase cytoplasmic;
DE EC=3.1.2.6 {ECO:0000269|PubMed:11085979, ECO:0000269|PubMed:19834746};
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
GN Name=GLX2-2; Synonyms=GLY2; OrderedLocusNames=At3g10850; ORFNames=T7M13.7;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9065762; DOI=10.1042/bj3220449;
RA Ridderstroem M., Mannervik B.;
RT "Molecular cloning and characterization of the thiolesterase glyoxalase II
RT from Arabidopsis thaliana.";
RL Biochem. J. 322:449-454(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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).
RN [6]
RP MUTAGENESIS OF HIS-54; ASP-58; CYS-142; LYS-144; ASN-180; ARG-227 AND
RP ARG-250, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=11085979; DOI=10.1074/jbc.m005090200;
RA Zang T.M., Hollman D.A., Crawford P.A., Crowder M.W., Makaroff C.A.;
RT "Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that
RT is essential for substrate binding and catalysis.";
RL J. Biol. Chem. 276:4788-4795(2001).
RN [7]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14529289; DOI=10.1021/bi034672o;
RA Schilling O., Wenzel N., Naylor M., Vogel A., Crowder M.W., Makaroff C.A.,
RA Meyer-Klaucke W.;
RT "Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II
RT incorporates iron, manganese, and zinc in vivo.";
RL Biochemistry 42:11777-11786(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=19834746; DOI=10.1007/s00775-009-0593-6;
RA Limphong P., McKinney R.M., Adams N.E., Makaroff C.A., Bennett B.,
RA Crowder M.W.;
RT "The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic
RT activity.";
RL J. Biol. Inorg. Chem. 15:249-258(2010).
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
CC {ECO:0000269|PubMed:11085979, ECO:0000269|PubMed:14529289,
CC ECO:0000269|PubMed:19834746}.
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 Evidence={ECO:0000269|PubMed:11085979, ECO:0000269|PubMed:19834746};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19834746};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19834746};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:19834746};
CC Note=Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit, catalysis
CC is optimal with 1 Fe and 1 Zn. Electron spin resonance indicates the
CC presence of a mixture of protein molecules that contain either Fe(2+)
CC or Fe(3+) and Zn(2+). Mn(2+) is not a cofactor (PubMed:19834746).
CC {ECO:0000269|PubMed:19834746};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=220 uM for S-D-lactoylglutathion {ECO:0000269|PubMed:14529289};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Mainly expressed in flowers and flower buds. Also
CC detected in roots and 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; U90929; AAC49867.1; -; mRNA.
DR EMBL; Y08357; CAA69644.1; -; mRNA.
DR EMBL; AC011708; AAF19564.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74963.1; -; Genomic_DNA.
DR EMBL; AY052329; AAK96522.1; -; mRNA.
DR EMBL; BT000849; AAN38686.1; -; mRNA.
DR RefSeq; NP_187696.1; NM_111922.4.
DR AlphaFoldDB; O24496; -.
DR SMR; O24496; -.
DR BioGRID; 5589; 3.
DR STRING; 3702.AT3G10850.1; -.
DR iPTMnet; O24496; -.
DR PaxDb; O24496; -.
DR PRIDE; O24496; -.
DR ProteomicsDB; 248584; -.
DR EnsemblPlants; AT3G10850.1; AT3G10850.1; AT3G10850.
DR GeneID; 820255; -.
DR Gramene; AT3G10850.1; AT3G10850.1; AT3G10850.
DR KEGG; ath:AT3G10850; -.
DR Araport; AT3G10850; -.
DR TAIR; locus:2103232; AT3G10850.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_030571_4_0_1; -.
DR InParanoid; O24496; -.
DR OMA; NYIWLLQ; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; O24496; -.
DR BRENDA; 3.1.2.6; 399.
DR SABIO-RK; O24496; -.
DR UniPathway; UPA00619; UER00676.
DR PRO; PR:O24496; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O24496; baseline and differential.
DR Genevisible; O24496; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase 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; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
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 PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Iron; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..258
FT /note="Hydroxyacylglutathione hydrolase cytoplasmic"
FT /id="PRO_0000192347"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 112
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 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 144..146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 174..176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT MUTAGEN 54
FT /note="H->N: Binds normal amount of metal, but reduced
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:11085979"
FT MUTAGEN 58
FT /note="D->C: Binds normal amount of metal, but reduced
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:11085979"
FT MUTAGEN 142
FT /note="C->A: Increases the metal content and the enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:11085979"
FT MUTAGEN 144
FT /note="K->A: Binds normal amount of metal, but reduced
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:11085979"
FT MUTAGEN 180
FT /note="N->A: 70% reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:11085979"
FT MUTAGEN 227
FT /note="R->A: Decreases metal binding and enzyme stability."
FT /evidence="ECO:0000269|PubMed:11085979"
FT MUTAGEN 250
FT /note="R->W: Decreases the substrate affinity."
FT /evidence="ECO:0000269|PubMed:11085979"
FT CONFLICT 14
FT /note="S -> T (in Ref. 1; AAC49867)"
FT /evidence="ECO:0000305"
FT CONFLICT 85..93
FT /note="GCTDAVDNG -> VALMRLIC (in Ref. 1; AAC49867)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..102
FT /note="LGQDI -> WSGY (in Ref. 1; AAC49867)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="N -> T (in Ref. 1; AAC49867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 28792 MW; 6703B98A8F902B5A CRC64;
MKIFHVPCLQ DNYSYLIIDE STGDAAVVDP VDPEKVIASA EKHQAKIKFV LTTHHHWDHA
GGNEKIKQLV PDIKVYGGSL DKVKGCTDAV DNGDKLTLGQ DINILALHTP CHTKGHISYY
VNGKEGENPA VFTGDTLFVA GCGKFFEGTA EQMYQSLCVT LAALPKPTQV YCGHEYTVKN
LEFALTVEPN NGKIQQKLAW ARQQRQADLP TIPSTLEEEL ETNPFMRVDK PEIQEKLGCK
SPIDTMREVR NKKDQWRG
