GLO2N_ARATH
ID GLO2N_ARATH Reviewed; 324 AA.
AC Q9SID3; Q3EBQ9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hydroxyacylglutathione hydrolase 2, mitochondrial;
DE EC=3.1.2.6;
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
DE Flags: Precursor;
GN OrderedLocusNames=At2g31350; ORFNames=T28P16.16;
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=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 [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 X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 72-324 IN COMPLEX WITH ZINC AND
RP IRON, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND COFACTOR.
RX PubMed=16227621; DOI=10.1074/jbc.m509748200;
RA Marasinghe G.P., Sander I.M., Bennett B., Periyannan G., Yang K.W.,
RA Makaroff C.A., Crowder M.W.;
RT "Structural studies on a mitochondrial glyoxalase II.";
RL J. Biol. Chem. 280:40668-40675(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 72-324 IN COMPLEX WITH ZINC AND
RP IRON.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
CC {ECO:0000269|PubMed:16227621}.
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:16227621};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:16227621};
CC Note=Binds 1 Fe(3+) ion per subunit. Electron spin resonance clearly
CC indicates the presence of Fe(3+) (PubMed:16227621).
CC {ECO:0000269|PubMed:16227621};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16227621};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16227621};
CC Note=Binds 1 Fe(2+) or Zn(2+) ion per subunit. Electron spin resonance
CC indicates the presence of either Fe(2+) or Zn(2+), while X-ray
CC crystallography shows the presence of Zn(2+). Mn(2+) is not a cofactor
CC (PubMed:16227621). {ECO:0000269|PubMed:16227621};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16227621,
CC ECO:0000269|PubMed:17850744}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SID3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SID3-2; Sequence=VSP_018092;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AC007169; AAD26483.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08531.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08532.1; -; Genomic_DNA.
DR EMBL; AY072200; AAL60021.1; -; mRNA.
DR EMBL; AY096672; AAM20306.1; -; mRNA.
DR PIR; F84719; F84719.
DR RefSeq; NP_180693.1; NM_128692.5. [Q9SID3-1]
DR RefSeq; NP_850166.1; NM_179835.1. [Q9SID3-2]
DR PDB; 1XM8; X-ray; 1.74 A; A/B=72-324.
DR PDB; 2Q42; X-ray; 1.74 A; A/B=72-324.
DR PDBsum; 1XM8; -.
DR PDBsum; 2Q42; -.
DR AlphaFoldDB; Q9SID3; -.
DR SMR; Q9SID3; -.
DR STRING; 3702.AT2G31350.1; -.
DR PaxDb; Q9SID3; -.
DR PRIDE; Q9SID3; -.
DR ProteomicsDB; 247396; -. [Q9SID3-1]
DR EnsemblPlants; AT2G31350.1; AT2G31350.1; AT2G31350. [Q9SID3-1]
DR EnsemblPlants; AT2G31350.2; AT2G31350.2; AT2G31350. [Q9SID3-2]
DR GeneID; 817693; -.
DR Gramene; AT2G31350.1; AT2G31350.1; AT2G31350. [Q9SID3-1]
DR Gramene; AT2G31350.2; AT2G31350.2; AT2G31350. [Q9SID3-2]
DR KEGG; ath:AT2G31350; -.
DR Araport; AT2G31350; -.
DR TAIR; locus:2061270; AT2G31350.
DR eggNOG; KOG0813; Eukaryota.
DR InParanoid; Q9SID3; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q9SID3; -.
DR BRENDA; 3.1.2.6; 399.
DR UniPathway; UPA00619; UER00676.
DR EvolutionaryTrace; Q9SID3; -.
DR PRO; PR:Q9SID3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SID3; baseline and differential.
DR Genevisible; Q9SID3; AT.
DR GO; GO:0005739; C:mitochondrion; NAS:TAIR.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:TAIR.
DR GO; GO:0005506; F:iron ion binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
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 SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Iron; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 65..324
FT /note="Hydroxyacylglutathione hydrolase 2, mitochondrial"
FT /id="PRO_0000012287"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:16227621,
FT ECO:0000269|PubMed:17850744"
FT VAR_SEQ 19
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018092"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1XM8"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1XM8"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:1XM8"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1XM8"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:1XM8"
SQ SEQUENCE 324 AA; 35841 MW; 91F47F391EFB0AE1 CRC64;
MQTISKASSA TSFFRCSRKL SSQPCVRQLN IRKSLVCRVM KLVSSPLRTL RGAGKSIRVS
KFCSVSNVSS LQIELVPCLK DNYAYILHDE DTGTVGVVDP SEAEPIIDSL KRSGRNLTYI
LNTHHHYDHT GGNLELKDRY GAKVIGSAMD KDRIPGIDMA LKDGDKWMFA GHEVHVMDTP
GHTKGHISLY FPGSRAIFTG DTMFSLSCGK LFEGTPKQML ASLQKITSLP DDTSIYCGHE
YTLSNSKFAL SLEPNNEVLQ SYAAHVAELR SKKLPTIPTT VKMEKACNPF LRSSNTDIRR
ALRIPEAADE AEALGIIRKA KDDF
