(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 96.
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}.
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   SMR; Q8ZRM2; -.
DR   PaxDb; Q8ZRM2; -.
DR   PRIDE; Q8ZRM2; -.
DR   EnsemblBacteria; AAL19218; AAL19218; STM0261.
DR   GeneID; 1251779; -.
DR   KEGG; stm:STM0261; -.
DR   PATRIC; fig|99287.12.peg.270; -.
DR   eggNOG; ENOG4108RW0; Bacteria.
DR   eggNOG; COG0491; LUCA.
DR   HOGENOM; HOG000058041; -.
DR   KO; K01069; -.
DR   OMA; NYIWLLQ; -.
DR   PhylomeDB; Q8ZRM2; -.
DR   BioCyc; SENT99287:STM0261-MONOMER; -.
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;
DR   PRODOM; Q8ZRM2.
DR   SWISS-2DPAGE; Q8ZRM2.
KW   3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..251
FT                   /note="Hydroxyacylglutathione hydrolase"
FT                   /id="PRO_0000309704"
FT   METAL           53
FT                   /note="Divalent metal cation 1; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           55
FT                   /note="Divalent metal cation 1; via pros nitrogen"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           57
FT                   /note="Divalent metal cation 2"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           58
FT                   /note="Divalent metal cation 2; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           110
FT                   /note="Divalent metal cation 1; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           127
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           127
FT                   /note="Divalent metal cation 2"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   METAL           165
FT                   /note="Divalent metal cation 2; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:17764159"
FT   STRAND          2..8
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   TURN            9..11
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          12..18
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          22..27
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           32..42
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          45..50
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           56..59
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           62..68
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          73..76
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           78..83
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          86..88
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          94..97
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          100..106
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          109..111
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          115..119
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          122..126
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          138..140
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           142..153
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   STRAND          160..165
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           168..178
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           183..197
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           207..213
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           215..217
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           222..229
FT                   /evidence="ECO:0000244|PDB:2QED"
FT   HELIX           237..250
FT                   /evidence="ECO:0000244|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
//

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