ID   STHA_AZOVI              Reviewed;         464 AA.
AC   Q9XBQ9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 114.
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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC   102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX   PubMed=11004404; DOI=10.1111/j.1574-6968.2000.tb09323.x;
RA   Boonstra B., Bjorklund L., French C.E., Wainwright I., Bruce N.C.;
RT   "Cloning of the sth gene from Azotobacter vinelandii and construction of
RT   chimeric soluble pyridine nucleotide transhydrogenases.";
RL   FEMS Microbiol. Lett. 191:87-93(2000).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC   102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX   PubMed=7460901; DOI=10.1111/j.1432-1033.1980.tb04948.x;
RA   Voordouw G., van der Vies S.M., Eweg J.K., Veeger C., van Breemen J.F.L.,
RA   van Bruggen E.F.J.;
RT   "Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved
RT   purification, physical properties and subunit arrangement in purified
RT   polymers.";
RL   Eur. J. Biochem. 111:347-355(1980).
RN   [3]
RP   SUBUNIT.
RC   STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC   102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX   PubMed=39756; DOI=10.1111/j.1432-1033.1979.tb13205.x;
RA   Voordouw G., Veeger C., van Breemen J.F.L., van Bruggen E.F.J.;
RT   "Structure of pyridine nucleotide transhydrogenase from Azotobacter
RT   vinelandii.";
RL   Eur. J. Biochem. 98:447-454(1979).
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;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- SUBUNIT: Homooctamer. Forms a polymeric filamentous structure in
CC       purified form. {ECO:0000269|PubMed:39756}.
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; AF159108; AAD40691.1; -; Genomic_DNA.
DR   RefSeq; WP_012700102.1; NZ_FPKM01000023.1.
DR   AlphaFoldDB; Q9XBQ9; -.
DR   SMR; Q9XBQ9; -.
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; FAD; Flavoprotein; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..464
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_0000068060"
FT   BINDING         35..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  51331 MW;  B67F2A3365CE0781 CRC64;
     MAVYNYDVVV IGTGPAGEGA AMNAVKAGRK VAVVDDRPQV GGNCTHLGTI PSKALRHSVR
     QIMQYNNNPL FRQIGEPRWF SFADVLKSAE QVIAKQVSSR TGYYARNRID TFFGTASFCD
     EHTIEVVHLN GMVETLVAKQ FVIATGSRPY RPADVDFTHP RIYDSDTILS LGHTPRRLII
     YGAGVIGCEY ASIFSGLGVL VDLIDNRDQL LSFLDDEISD SLSYHLRNNN VLIRHNEEYE
     RVEGLDNGVI LHLKSGKKIK ADAFLWSNGR TGNTDKLGLE NIGLKANGRG QIQVDEHYRT
     EVSNIYAAGD VIGWPSLASA AYDQGRSAAG SITENDSWRF VDDVPTGIYT IPEISSVGKT
     ERELTQAKVP YEVGKAFFKG MARAQIAVEK AGMLKILFHR ETLEILGVHC FGYQASEIVH
     IGQAIMNQKG EANTLKYFIN TTFNYPTMAE AYRVAAYDGL NRLF