ID STHA_PSEPF Reviewed; 464 AA. AC Q3K9F5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 39. 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=Pfl01_3862; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA75599.1; -; Genomic_DNA. DR RefSeq; YP_349590.1; -. DR GeneID; 3712292; -. DR GenomeReviews; CP000094_GR; Pfl01_3862. DR KEGG; pfo:Pfl01_3862; -. DR HOGENOM; Q3K9F5; -. DR OMA; Q3K9F5; EVVCANG. DR BioCyc; PFLU205922:PFL_3862-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_0000260239. FT NP_BIND 35 44 FAD (By similarity). SQ SEQUENCE 464 AA; 50891 MW; BB34A1B3B5826D16 CRC64; MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVR QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVISKQVASR TGYYARNRVD VFFGTGSFAD EQTIEVVCAN GVVEKLVAKH IIIATGSRPY RPADIDFHHP RIYDSDTILS LGHTPRKLIV YGAGVIGCEY ASIFSGLGVL VELVDNRGQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYD RVEGVDNGVI LHLKSGKKIK ADALLWCNGR TGNTDQLGLE NIGVKVNSRG QIEVDENYRT CVQNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRF VNDVPTGIYT IPEISSIGKN EQELTQAKVP YEVGKAFFKS MARAQIAGEP QGMLKILFHR ETLEVLGVHC FGYQASEIVH IGQAIMNQPG ELNTLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF //