ID   STHA_PROMH              Reviewed;         465 AA.
AC   B4F1H1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000255|HAMAP-Rule:MF_00247};
DE            Short=STH {ECO:0000255|HAMAP-Rule:MF_00247};
DE            EC=1.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00247};
DE   AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000255|HAMAP-Rule:MF_00247};
GN   Name=sthA {ECO:0000255|HAMAP-Rule:MF_00247};
GN   Synonyms=udhA {ECO:0000255|HAMAP-Rule:MF_00247}; OrderedLocusNames=PMI3242;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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:0000255|HAMAP-Rule:MF_00247}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + NADPH = NADH + NADP(+); Xref=Rhea:RHEA:11692,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58349; EC=1.6.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00247};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00247};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00247};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00247}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000255|HAMAP-Rule:MF_00247}.
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DR   EMBL; AM942759; CAR46348.1; -; Genomic_DNA.
DR   RefSeq; WP_004246384.1; NC_010554.1.
DR   AlphaFoldDB; B4F1H1; -.
DR   SMR; B4F1H1; -.
DR   STRING; 529507.PMI3242; -.
DR   EnsemblBacteria; CAR46348; CAR46348; PMI3242.
DR   GeneID; 6800710; -.
DR   KEGG; pmr:PMI3242; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   OMA; CLMAVGA; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006739; P:NADP metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00247; SthA; 1.
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   InterPro; IPR022962; STH.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..465
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_1000100857"
FT   BINDING         35..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00247"
SQ   SEQUENCE   465 AA;  51394 MW;  290873589266A035 CRC64;
     MQHSHFDAIV IGSGPGGEGA AMGLVKQGKR VAVIERYDQV GGGCTHWGTI PSKALRHAVS
     RIIEFNQNPL YSDQSRLINS SFSQILRQAS TVISQQTKMR QGFYERNHCT MYSGEAAFID
     DHRISVRYPD GTCDILSADN FIIATGSRPY CPPDVDFSHS RIYNSDTILD LEHEPRHVII
     YGAGVIGCEY ASIFRGLRVK VDLINTRDHL LSFLDQEMSD ALSYHFWNNG IVIRHNEEYD
     TIEGVDDGVI VHLKSGKKVK ADCLLYANGR TGNTDTLGLE NVGIKTDSRG QVAVNAHYQT
     SCEHIYAVGD VIGYPSLASA AYDQGRIAAL ALTTGTSETH LIEDIPTGIY TIPEISSVGK
     TEQQLTAMKI PYEVGRSQFK HLARAQIAGM NVGSLKILFH RETKQILGIH CFGERAAEII
     HIGQAIMEQK GEGNTIEYFV NTTFNYPTMA EAYRVAALNG LNRLF