ID   B0STZ5_LEPBP            Unreviewed;       480 AA.
AC   B0STZ5;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 111.
DE   RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000256|ARBA:ARBA00016603};
DE            EC=1.6.1.1 {ECO:0000256|ARBA:ARBA00012772};
DE   AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000256|ARBA:ARBA00031183};
GN   OrderedLocusNames=LEPBI_II0144 {ECO:0000313|EMBL:ABZ99679.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Pseudomonadati; Spirochaetota; Leptospiria; Leptospirales;
OC   Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99679.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ99679.1, 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   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for energy
CC       generation. {ECO:0000256|ARBA:ARBA00002842}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR   EMBL; CP000787; ABZ99679.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0STZ5; -.
DR   STRING; 456481.LEPBI_II0144; -.
DR   KEGG; lbi:LEPBI_II0144; -.
DR   HOGENOM; CLU_016755_0_0_12; -.
DR   Proteomes; UP000001847; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase (NADH) activity; IEA:TreeGrafter.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:TreeGrafter.
DR   GO; GO:0003957; F:NAD(P)+ transhydrogenase (Si-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:TreeGrafter.
DR   FunFam; 3.30.390.30:FF:000001; Dihydrolipoyl dehydrogenase; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR050151; Class-I_Pyr_Nuc-Dis_Oxidored.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   NCBIfam; NF003585; PRK05249.1; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR22912:SF93; SOLUBLE PYRIDINE NUCLEOTIDE TRANSHYDROGENASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABZ99679.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          20..343
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          364..471
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         66
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         130
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         159..161
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         198..205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ   SEQUENCE   480 AA;  52784 MW;  8CACAE5EAD8BA04F CRC64;
     MLFFTLSVAF FYPMSINRFD LIAIGGGPAA QKAAIQASKL GKKAAIIEKD PYLGGGCVHW
     GTIPSKSLQE TSRFYRNLKL SNLHGLQSPQ TAQLTLQELM FRAGTVIEKE EDVTREQMIQ
     NRVTTLTGWG KIIDKNQVEV TDSAGRKKVY ETENILIATG SSPRRPTNEN IPFEEGLVYD
     SDGLFAMKKM PRTLAVIGAG IIGSEYATIF AHIGVKVHLF DSQSRILGFL DEDISNEMTR
     IMQNAGIQIH VDSSITSYQK ISEETGFQLT TNKGEVITVN QVLISRGRLG NVDNLGLEAV
     GILPNDRKQI QVNENYQTNI PNIYACGDVI GFPSLASVSM YQGAYVAKHM FGLPSVPVDA
     EEFPIGIYTL PEIATIGPTE EALKKRGVPY GVGLAKFDTI TRAQISGDQV GLLKILFDKQ
     TRRVLGVHII SDKATELIAL GQCVVNLKAP IEYFTEHIFN YPTMIGAYKN AANDALLREK
//