ID   STHA_PSEU2              Reviewed;         464 AA.
AC   Q4ZV77;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=Psyr_1901;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY36945.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000075; AAY36945.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003436620.1; NC_007005.1.
DR   RefSeq; YP_234983.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZV77; -.
DR   SMR; Q4ZV77; -.
DR   STRING; 205918.Psyr_1901; -.
DR   PRIDE; Q4ZV77; -.
DR   EnsemblBacteria; AAY36945; AAY36945; Psyr_1901.
DR   KEGG; psb:Psyr_1901; -.
DR   PATRIC; fig|205918.7.peg.1945; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   Proteomes; UP000000426; 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..464
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_0000260241"
FT   BINDING         35..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00247"
SQ   SEQUENCE   464 AA;  50783 MW;  21CFE19287233998 CRC64;
     MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVK
     QIIQFNTNPM FRAIGEPRWF SFPDVLKNAE MVISKQVASR TSYYARNRVD VFFGTGSFAD
     ETSINVVCTN GVVEKLVANQ IIIATGSRPY RPADIDFSHK RIYDSDTILS LGHTPRKLII
     YGAGVIGCEY ASIFSGLGVL VELVDNRDQL LSFLDSEISQ ALSYHFSNNN VMVRHNEEYE
     KVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NIGLKANGRG QIEVDETYRT
     SVSNVYGAGD VIGWPSLASA AYDQGRSAAG SMVDNGSWRY VNDVPTGIYT IPEISSIGKN
     EHELTQAKVP YEVGKAFFKG MARAQISGER VGMLKILFHR ETLEVLGVHC FGDQASEIVH
     IGQAIMSQPG EANTMKYFVN TTFNYPTMAE AYRVAAYDGL NRLF