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Database: UniProt
Entry: B0SLG6_LEPBP
LinkDB: B0SLG6_LEPBP
Original site: B0SLG6_LEPBP 
ID   B0SLG6_LEPBP            Unreviewed;       324 AA.
AC   B0SLG6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:ABZ98552.1};
DE            EC=1.1.1.169 {ECO:0000313|EMBL:ABZ98552.1};
GN   Name=panE {ECO:0000313|EMBL:ABZ98552.1};
GN   OrderedLocusNames=LEPBI_I2463 {ECO:0000313|EMBL:ABZ98552.1};
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:ABZ98552.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ98552.1, 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).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; CP000786; ABZ98552.1; -; Genomic_DNA.
DR   RefSeq; WP_012389413.1; NC_010602.1.
DR   AlphaFoldDB; B0SLG6; -.
DR   STRING; 456481.LEPBI_I2463; -.
DR   KEGG; lbi:LEPBI_I2463; -.
DR   HOGENOM; CLU_031468_0_0_12; -.
DR   OrthoDB; 9793586at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS12155-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:ABZ98552.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          8..153
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          180..319
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   324 AA;  36484 MW;  7241B2430660BA61 CRC64;
     MNDFFPSIAI CGIGSVTVTI VHAFHQNKVP FKILCKDQTR FDFLKEKPIQ FKDPDGKIIK
     IDLGDHLTLI QDSKDKFDFI FLGCKNQSLN EYLSITENAL DSNGKWILIQ NGLPETHFPN
     LMEKLIGGVV GWNTQVLSDG TYFQSNPGSL ILGGCNQTKL NPIWPSLLHP WIEVKLTEEI
     LGYRWHKLAI NAIINGLAAS KQLSLGQLFL NEEGRKEAIS ILTEVKQLMF FLKIKEGVVP
     GSVPIHKLGD GKGALPVWIR HLILIFLGLK YFKIRTSMVQ DLDHKRKTEI NYINGEIVKI
     AGLHKIPVPA NLKVLNEVLK LESE
//
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