GLO2_SALTY
ID GLO2_SALTY Reviewed; 251 AA.
AC Q8ZRM2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Hydroxyacylglutathione hydrolase;
DE EC=3.1.2.6;
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
GN Name=gloB; OrderedLocusNames=STM0261;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, COFACTOR, SUBUNIT, STRUCTURE BY NMR, AND X-RAY CRYSTALLOGRAPHY
RP (1.45 ANGSTROMS).
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=17764159; DOI=10.1021/bi7007245;
RA Campos-Bermudez V.A., Leite N.R., Krog R., Costa-Filho A.J., Soncini F.C.,
RA Oliva G., Vila A.J.;
RT "Biochemical and structural characterization of Salmonella typhimurium
RT glyoxalase II: new insights into metal ion selectivity.";
RL Biochemistry 46:11069-11079(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:17764159}.
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:0000269|PubMed:17764159};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17764159};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17764159};
CC Note=Binds 2 metal ions per subunit; upon overexpression in E.coli the
CC enzyme purifies with various amounts of iron, zinc and manganese. The
CC endogenous metal is unknown. {ECO:0000269|PubMed:17764159};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17764159}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AE006468; AAL19218.1; -; Genomic_DNA.
DR RefSeq; NP_459259.1; NC_003197.2.
DR RefSeq; WP_001052775.1; NC_003197.2.
DR PDB; 2QED; X-ray; 1.45 A; A=1-251.
DR PDBsum; 2QED; -.
DR AlphaFoldDB; Q8ZRM2; -.
DR SMR; Q8ZRM2; -.
DR STRING; 99287.STM0261; -.
DR PaxDb; Q8ZRM2; -.
DR EnsemblBacteria; AAL19218; AAL19218; STM0261.
DR GeneID; 1251779; -.
DR KEGG; stm:STM0261; -.
DR PATRIC; fig|99287.12.peg.270; -.
DR HOGENOM; CLU_030571_4_1_6; -.
DR OMA; NYIWLLQ; -.
DR PhylomeDB; Q8ZRM2; -.
DR BioCyc; SENT99287:STM0261-MON; -.
DR BRENDA; 3.1.2.6; 5542.
DR SABIO-RK; Q8ZRM2; -.
DR UniPathway; UPA00619; UER00676.
DR EvolutionaryTrace; Q8ZRM2; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-UniRule.
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 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..251
FT /note="Hydroxyacylglutathione hydrolase"
FT /id="PRO_0000309704"
FT BINDING 53
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 55
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 110
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17764159"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17764159"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2QED"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:2QED"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:2QED"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:2QED"
SQ SEQUENCE 251 AA; 28633 MW; 5A8194A0C921C0E9 CRC64;
MNLNSIPAFQ DNYIWVLTND EGRCVIVDPG EAAPVLKAIA EHKWMPEAIF LTHHHHDHVG
GVKELLQHFP QMTVYGPAET QDKGATHLVG DGDTIRVLGE KFTLFATPGH TLGHVCYFSR
PYLFCGDTLF SGGCGRLFEG TPSQMYQSLM KINSLPDDTL ICCAHEYTLA NIKFALSILP
HDSFINEYYR KVKELRVKKQ MTLPVILKNE RKINLFLRTE DIDLINEINK ETILQQPEAR
FAWLRSKKDT F
