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Database: UniProt
Entry: B0SQE1_LEPBP
LinkDB: B0SQE1_LEPBP
Original site: B0SQE1_LEPBP 
ID   B0SQE1_LEPBP            Unreviewed;       153 AA.
AC   B0SQE1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Putative lactoylglutathione lyase {ECO:0000313|EMBL:ABZ97599.1};
DE            EC=4.4.1.5 {ECO:0000313|EMBL:ABZ97599.1};
GN   OrderedLocusNames=LEPBI_I1492 {ECO:0000313|EMBL:ABZ97599.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97599.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ97599.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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DR   EMBL; CP000786; ABZ97599.1; -; Genomic_DNA.
DR   RefSeq; WP_012388478.1; NC_010602.1.
DR   AlphaFoldDB; B0SQE1; -.
DR   STRING; 456481.LEPBI_I1492; -.
DR   KEGG; lbi:LEPBI_I1492; -.
DR   HOGENOM; CLU_110049_0_0_12; -.
DR   OrthoDB; 332982at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS07330-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR037523; VOC.
DR   PANTHER; PTHR43048; METHYLMALONYL-COA EPIMERASE; 1.
DR   PANTHER; PTHR43048:SF3; METHYLMALONYL-COA EPIMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF13669; Glyoxalase_4; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ABZ97599.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          9..135
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
SQ   SEQUENCE   153 AA;  16999 MW;  DDC333DD0C8B468E CRC64;
     MSRPFKVLGI QQVAIGGESK EKLSKFWVEI MGLTKVSDYK SEKENVDEDI LSMGNGPYKV
     EIDLMQPIDP NKSPKVHDPK LNHIGLWIDK LEECVDYLTK QGVRFTPGGI RKGAAGYNVC
     FIHPKGNEEF PLCSEGVLVE LVQAPEDVIK ALG
//
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