ID GLO2_NOSP7 Reviewed; 257 AA.
AC B2IVH7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Hydroxyacylglutathione hydrolase;
DE EC=3.1.2.6;
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
GN Name=gloB; OrderedLocusNames=Npun_F2829;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M.,
RA Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-
CC lactoyl-glutathione to form glutathione and D-lactic acid (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: S-(2-hydroxyacyl)glutathione + H(2)O =
CC glutathione + a 2-hydroxy carboxylate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC degradation; (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family.
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DR EMBL; CP001037; ACC81362.1; -; Genomic_DNA.
DR RefSeq; YP_001866305.1; NC_010628.1.
DR ProteinModelPortal; B2IVH7; -.
DR STRING; 63737.Npun_F2829; -.
DR EnsemblBacteria; ACC81362; ACC81362; Npun_F2829.
DR GeneID; 6252240; -.
DR KEGG; npu:Npun_F2829; -.
DR PATRIC; 22758288; VBINosPun48114_3309.
DR eggNOG; COG0491; -.
DR HOGENOM; HOG000058041; -.
DR KO; K01069; -.
DR OMA; LTHHHQD; -.
DR ProtClustDB; CLSK892602; -.
DR BioCyc; NPUN63737:GJNP-2764-MONOMER; -.
DR UniPathway; UPA00619; UER00676.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:InterPro.
DR HAMAP; MF_01374; Glyoxalase_2; 1; -.
DR InterPro; IPR001279; Beta-lactamas-like.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR PANTHER; PTHR11935:SF7; PTHR11935:SF7; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 3: Inferred from homology;
KW Complete proteome; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1 257 Hydroxyacylglutathione hydrolase.
FT /FTId=PRO_1000144776.
FT METAL 54 54 Zinc 1 (By similarity).
FT METAL 56 56 Zinc 1 (By similarity).
FT METAL 58 58 Zinc 2 (By similarity).
FT METAL 59 59 Zinc 2 (By similarity).
FT METAL 113 113 Zinc 1 (By similarity).
FT METAL 137 137 Zinc 1 (By similarity).
FT METAL 137 137 Zinc 2 (By similarity).
FT METAL 175 175 Zinc 2 (By similarity).
SQ SEQUENCE 257 AA; 28966 MW; C42B006FF2B7613B CRC64;
MQVIRLEALS DNYIFLLYDD KRNIAAVVDP AEAQPVLKKL AELKADLVAI FNTHHHNDHV
GGNKQLIEKF PQLIVYGGAE DRGRIPGQKV FLQQGDRVEF ADRIAEVIFV PGHTRAHIAY
YFPPQEASET GDLFCGDTLF SGGCGRLFEG TPTQMVDSLS KLRSLPDNTR IWCAHEYTLK
NLQFALTVDG DNADLQRRFN EVKAYRSRGE ATIPSLLGVE KHTNPFLRWD QASLQSTVKS
SDGVQTFARI REMKNNF
//
