ID   STHA_PSEF5              Reviewed;         464 AA.
AC   Q4KFA6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
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; OrderedLocusNames=PFL_1958;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
CC   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for
CC       energy generation (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; CP000076; AAY91245.1; -; Genomic_DNA.
DR   RefSeq; YP_259077.1; -.
DR   GeneID; 3478078; -.
DR   GenomeReviews; CP000076_GR; PFL_1958.
DR   KEGG; pfl:PFL_1958; -.
DR   NMPDR; fig|220664.3.peg.3398; -.
DR   HOGENOM; Q4KFA6; -.
DR   OMA; Q4KFA6; EVVCANG.
DR   BioCyc; PFLU220664:PFL_1958-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:HAMAP.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006739; P:NADP metabolic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00247; -; 1.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    464       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000260238.
FT   NP_BIND      35     44       FAD (By similarity).
SQ   SEQUENCE   464 AA;  50757 MW;  9D0C53267E4AB383 CRC64;
     MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVR
     QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVISKQVASR TGYYARNRVD VFFGTGSFAD
     EQTVEVVCAN GVVEKLVAKH IIIATGSRPY RPADIDFSHP RIYDSDTILS LGHTPRKLIV
     YGAGVIGCEY ASIFSGLGVL VELVDNRGQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYD
     RVEGVDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGME NIGVKVNSRG QIEVDENYRT
     CVPNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRF VNDVPTGIYT IPEISSIGKN
     EQELTQAKVP YEVGKAFFKG MARAQIAGEP QGMLKILFHR ETLEVLGVHC FGYQASEIVH
     IGQAIMSQPG ELNTLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF
//