ID   STHA_YERPS              Reviewed;         466 AA.
AC   Q66G61;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
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};
GN   OrderedLocusNames=YPTB0121;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19361.1; -; Genomic_DNA.
DR   RefSeq; WP_002209477.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66G61; -.
DR   SMR; Q66G61; -.
DR   EnsemblBacteria; CAH19361; CAH19361; YPTB0121.
DR   GeneID; 66843486; -.
DR   KEGG; ypo:BZ17_2476; -.
DR   KEGG; yps:YPTB0121; -.
DR   PATRIC; fig|273123.14.peg.2594; -.
DR   OMA; CLMAVGA; -.
DR   Proteomes; UP000001011; 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.
FT   CHAIN           1..466
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_0000260248"
FT   BINDING         36..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00247"
SQ   SEQUENCE   466 AA;  51382 MW;  D6CD965D6CF3E2CE CRC64;
     MQQHFHFDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYNN VGGGCTHWGT IPSKALRHAV
     SRIIEFNQNP LYSDNARTIK SSFADILNHA DRVINQQTRM RQGFYDRNHC HMFSGDASFI
     DANTVNVRYA DGTSDTLQAD NIVIATGSRP YRPVNVDFNH ERIYDSDTIL QLSHEPQHVI
     IYGAGVIGCE YASIFRGLSV KVDLINTRDR LLAFLDQEMS DALSYHFWNN GVVIRHNEEF
     EQIEGTTDGV IVHLKSGKKV KADCLLYANG RTGNTSGLGL ENIGLEADSR GLLKVNSMYQ
     TALSHVYAVG DVIGYPSLAS AAYDQGRIAA QAMIKGEANV HLIEDIPTGI YTIPEISSVG
     KTEQELTAMK VPYEVGRAQF KHLARAQIVG MDTGSLKILF HRETKQILGI HCFGERAAEI
     IHIGQAIMEQ KGEGNTLEYF VNTTFNYPTM AEAYRVAALN GLNRLF