ID   STHA_VIBCH              Reviewed;         466 AA.
AC   P50529;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Soluble pyridine nucleotide transhydrogenase;
DE            Short=STH;
DE            EC=1.6.1.1;
DE   AltName: Full=NAD(P)(+) transhydrogenase [B-specific];
GN   Name=sthA; Synonyms=udhA; OrderedLocusNames=VC_0151;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 421-466.
RC   STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX   PubMed=9168128; DOI=10.1016/s0378-1119(96)00849-9;
RA   Sahu G.K., Chowdhury R., Das J.;
RT   "The rpoH gene encoding sigma 32 homolog of Vibrio cholerae.";
RL   Gene 189:203-207(1997).
CC   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for energy
CC       generation. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF93328.1; -; Genomic_DNA.
DR   EMBL; U44432; AAC45342.1; -; Genomic_DNA.
DR   PIR; E82357; E82357.
DR   RefSeq; NP_229809.1; NC_002505.1.
DR   RefSeq; WP_000529898.1; NZ_LT906614.1.
DR   AlphaFoldDB; P50529; -.
DR   SMR; P50529; -.
DR   STRING; 243277.VC_0151; -.
DR   DNASU; 2614850; -.
DR   EnsemblBacteria; AAF93328; AAF93328; VC_0151.
DR   GeneID; 57741355; -.
DR   KEGG; vch:VC_0151; -.
DR   PATRIC; fig|243277.26.peg.139; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   OMA; CLMAVGA; -.
DR   BioCyc; VCHO:VC0151-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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..466
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_0000068075"
FT   BINDING         36..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  50942 MW;  60D05DB3FD595BE1 CRC64;
     MGQKNHFDVI VIGSGPGGEG AAMGLTKGGK NVAIIEKESS VGGGCTHWGT IPSKALRHAV
     SRIIEFNSNP LFCKNNSSIH ATFSTILSHA KSVIDKQTRL RQGFYDRNQC TLIFGAAHFI
     DAHTVAVKKA DGSIDTYSAD KFVIATGSRP YHPKDVDFGH PRIYDSDSIL NLEHDPRHII
     IYGAGVIGCE YASIFRGLDV KTDLINTRDR LLSFLDNEVS DALSYHFWNS GVVIRNDETY
     DKVEGTSDGV IVHLKSGKKM RADCLLYANG RTGNTDKLNL ESVGLQADSR GQLVVNANYQ
     TQVEHIYAVG DVIGYPSLAS AAYDQGRFVA QAIIHGQAAH LLTEDIPTGI YTIPEISSVG
     RTEQELTAAK VPYEVGRASF KHLARAQIAG KDIGSLKILF HRETKEILGI HCFGERAAEI
     IHIGQAIMEQ KGEANTIEYF VNTTFNYPTM AEAFRVAALN GLNRLF