ID   STHA_PSEMY              Reviewed;         464 AA.
AC   A4XSQ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=Pmen_1603;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA   Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP84367.1; -; Genomic_DNA.
DR   RefSeq; YP_001187099.1; -.
DR   GeneID; 5109261; -.
DR   GenomeReviews; CP000680_GR; Pmen_1603.
DR   KEGG; pmy:Pmen_1603; -.
DR   OMA; A4XSQ1; GEGNTIE.
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_1000012564.
FT   NP_BIND      35     44       FAD (By similarity).
SQ   SEQUENCE   464 AA;  51015 MW;  7F403879A82E3C7F CRC64;
     MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAVVDNRPLV GGNCTHLGTI PSKALRHSVR
     QIMQFNTNPM FRQIGEPRWF SFPDVLKSAE KVIAKQVTSR TGYYARNRID TYFGTASFAD
     EQTVEVVCLN GVVEKLVAKQ IVIATGSRPY RPADVDFRHP RIYDSDTILS LGHTPRRLII
     YGAGVIGCEY ASIFSGLGVL VDLIDNRDQL LSFLDSEISD ALSYHLRNNN VLIRHNEEYE
     RIEGVENGVV LHLKSGKKIK ADALLWCNGR TGNTDQLGLE NIGIAVNSRG QIQVDEHYRT
     EVSNIYAAGD VIGWPSLASA AADQGRSAAG SIVENGSWRF VDDVPTGIYT IPEISSIGKT
     ERELTQAKVP YEVGKAFFKG MARAQISVEP VGMLKILFHR ETLEVLGVHC FGYQASEIVH
     IGQAIMNQKG EANSIKYFIN TTFNYPTMAE AYRVAAFDGL NRLF
//