ID I4B0V1_TURPD Unreviewed; 463 AA.
AC I4B0V1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=NAD(P)(+) transhydrogenase (Si-specific) {ECO:0000256|ARBA:ARBA00012772};
DE EC=1.6.1.1 {ECO:0000256|ARBA:ARBA00012772};
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000256|ARBA:ARBA00031183};
GN OrderedLocusNames=Turpa_0248 {ECO:0000313|EMBL:AFM10908.1};
OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS (Leptospira parva).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Turneriella.
OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM10908.1, ECO:0000313|Proteomes:UP000006048};
RN [1] {ECO:0000313|EMBL:AFM10908.1, ECO:0000313|Proteomes:UP000006048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC {ECO:0000313|Proteomes:UP000006048};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP002959; AFM10908.1; -; Genomic_DNA.
DR RefSeq; WP_014801429.1; NC_018020.1.
DR AlphaFoldDB; I4B0V1; -.
DR STRING; 869212.Turpa_0248; -.
DR KEGG; tpx:Turpa_0248; -.
DR PATRIC; fig|869212.3.peg.210; -.
DR HOGENOM; CLU_016755_0_0_12; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000006048; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 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|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
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 Reference proteome {ECO:0000313|Proteomes:UP000006048}.
FT DOMAIN 4..324
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 344..455
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 145..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 181..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 463 AA; 51062 MW; B74A6C6F5FD85900 CRC64;
MTRYDVVVIG SGPAGEGAAM QCAKDGKHTA IVELNETLGG ECLHRGTIPS KALRHSIQRY
IESMSNPLVK SHVNFASREL DFPQMLAAAR KIIEREAQHN LSYYERNRVD VYGGRARIVT
PNEIQIEMGQ RGTETIQADA IIVATGSRPY HPPDIKFDDH VLDSDTVLEL AYTPRSITIY
GAGVIGCEYA SIFKGLGIKV TLVNHRAKLL EFLDDEIIDA LSYHLREQGI VIKHGEEYEK
VERDGNEVQL HLKSGKIIKS EALLWANGRS GNSAGLFGFE SGIEIDHRGQ IKKNENFQTA
LPHIYAVGDV SGPPALASAA FNQGRFVALH ITRGTSFANL VQRIPTGIYT APEISSLGKT
ERELTAEKVP YEVGQAHFRN IARAQITGQT AGLLKILFHR ETLEILGIHC FGDQAAEIIH
IGQAIMSQPA PNNRVTWFVE TTFNYPTMAE AYRVAALNGI NRL
//
