ID   STHA_PSEFL              Reviewed;         464 AA.
AC   O05139;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 67.
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; Synonyms=sth;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, AND
RP   CHARACTERIZATION.
RC   STRAIN=NCIMB 9815;
RX   MEDLINE=97252509; PubMed=9098078;
RA   French C.E., Boonstra B., Bufton K.A.J., Bruce N.C.;
RT   "Cloning, sequence, and properties of the soluble pyridine nucleotide
RT   transhydrogenase of Pseudomonas fluorescens.";
RL   J. Bacteriol. 179:2761-2765(1997).
CC   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for
CC       energy generation.
CC   -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homooligomer; probably composed of four stacked rings of
CC       7 or 8 monomers. Forms filamentous structures.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; U91523; AAB50562.1; -; Genomic_DNA.
DR   HSSP; P14218; 1LPF.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
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   PRINTS; PR00411; PNDRDTASEI.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD; NADP;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    464       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000068069.
FT   NP_BIND      35     44       FAD (By similarity).
FT   CONFLICT     26     26       K -> D (in Ref. 1; AA sequence).
FT   CONFLICT     26     26       K -> R (in Ref. 1; AA sequence).
SQ   SEQUENCE   464 AA;  51008 MW;  333D7F4EABB6944F CRC64;
     MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVR
     QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVISKQVASR TGYYARNRVD LFFGTGSFAD
     EQTVEVVCAN GVVEKLVAKH IIIATGSRPY RPADIDFHHP RIYDSDTILS LGHTPRKLII
     YGAGVIGCEY ASIFSGLGVL VELVDNRDQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYD
     RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGME NIGVKVNSRG QIEVDENYRT
     CVTNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRY VNDVPTGIYT IPEISSIGKN
     EHELTKAKVP YEVGKAFFKS MARAQIAGEP QGMLKILFHR ETLEVLGVHC FGYQASEIVH
     IGQAIMNQPG EQNTLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF
//