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STHA_PSE14
ID   STHA_PSE14              Reviewed;         464 AA.
AC   Q48KI8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=PSPPH_1856;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(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}.
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DR   EMBL; CP000058; AAZ34919.1; -; Genomic_DNA.
DR   RefSeq; WP_004664563.1; NC_005773.3.
DR   AlphaFoldDB; Q48KI8; -.
DR   SMR; Q48KI8; -.
DR   STRING; 264730.PSPPH_1856; -.
DR   EnsemblBacteria; AAZ34919; AAZ34919; PSPPH_1856.
DR   KEGG; psp:PSPPH_1856; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   OMA; CLMAVGA; -.
DR   OrthoDB; 267896at2; -.
DR   Proteomes; UP000000551; 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_0000260240"
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;  50796 MW;  43D30E36C8D7E483 CRC64;
     MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVK
     QIIQFNTNPM FRAIGEPRWF SFPDVLKNAE MVISKQVASR TSYYARNRVD VFFGTGSFAD
     ETSVNVVCSN GVVEKLVANQ IIIATGSRPY RPADIDFSHK RIYDSDTILS LGHTPRKLII
     YGAGVIGCEY ASIFSGLGVL VELVDNRDQL LSFLDSEISQ ALSYHFSNNN VMVRHNEEYE
     RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NIGLKANGRG QIEVDENYRT
     SVSNVYGAGD VIGWPSLASA AYDQGRSAAG SMVDNGSWRY VNDVPTGIYT IPEISSIGKN
     EHELTQAKVP YEVGKAFFKG MARAQISGER VGMLKILFHR ETLEVLGVHC FGDQASEIVH
     IGQAIMSQPG EANTMKYFVN TTFNYPTMAE AYRVAAYDGL NRLF
 
 
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