ID   STHA_PSEFL              Reviewed;         464 AA.
AC   O05139;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 131.
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=sth;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, AND
RP   CHARACTERIZATION.
RC   STRAIN=NCIMB 9815 / KCTC 1767;
RX   PubMed=9098078; DOI=10.1128/jb.179.8.2761-2765.1997;
RA   French C.E., Boonstra B., Bufton K.A.J., Bruce N.C.;
RT   "Cloning, sequence, and properties of the soluble pyridine nucleotide
RT   transhydrogenase of Pseudomonas fluorescens.";
RL   J. Bacteriol. 179:2761-2765(1997).
CC   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for energy
CC       generation.
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   -!- SUBUNIT: Homooligomer; probably composed of four stacked rings of 7 or
CC       8 monomers. Forms filamentous structures.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; U91523; AAB50562.1; -; Genomic_DNA.
DR   RefSeq; WP_024074093.1; NZ_UGUS01000002.1.
DR   AlphaFoldDB; O05139; -.
DR   SMR; O05139; -.
DR   STRING; 690597.JH730961_gene4804; -.
DR   GeneID; 57518199; -.
DR   eggNOG; COG1249; Bacteria.
DR   OrthoDB; 267896at2; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD; NADP;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9098078"
FT   CHAIN           2..464
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_0000068069"
FT   BINDING         35..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        26
FT                   /note="K -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="K -> R (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  51008 MW;  333D7F4EABB6944F CRC64;
     MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVR
     QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVISKQVASR TGYYARNRVD LFFGTGSFAD
     EQTVEVVCAN GVVEKLVAKH IIIATGSRPY RPADIDFHHP RIYDSDTILS LGHTPRKLII
     YGAGVIGCEY ASIFSGLGVL VELVDNRDQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYD
     RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGME NIGVKVNSRG QIEVDENYRT
     CVTNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRY VNDVPTGIYT IPEISSIGKN
     EHELTKAKVP YEVGKAFFKS MARAQIAGEP QGMLKILFHR ETLEVLGVHC FGYQASEIVH
     IGQAIMNQPG EQNTLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF