ID   STHA_CHRSD              Reviewed;         463 AA.
AC   Q1QX78;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Csal_1577;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
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., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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; CP000285; ABE58930.1; -; Genomic_DNA.
DR   RefSeq; YP_573629.1; -.
DR   GeneID; 4027596; -.
DR   GenomeReviews; CP000285_GR; Csal_1577.
DR   KEGG; csa:Csal_1577; -.
DR   NMPDR; fig|290398.4.peg.2933; -.
DR   HOGENOM; Q1QX78; -.
DR   OMA; Q1QX78; EYFVENT.
DR   BioCyc; CSAL290398:CSAL_1577-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    463       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000260231.
FT   NP_BIND      35     44       FAD (By similarity).
SQ   SEQUENCE   463 AA;  51953 MW;  6442E282D3757021 CRC64;
     MAVHNFDVVV IGSGPAGESA AINAAKHGKR VAIVEKQQAV GGNCTHWGTI PSKALRHQVK
     QIMQFNTNRM FRDIGEPRWF SFPRVLERSK VTIDQQVEMR TQFYSRNRIN LFFGVARFRD
     EHTLTVRDNQ DGVEELCAQQ FVIATGSRPY RPADINFRHP RIYCSDTILG LSHTPRTLII
     FGAGVIGSEY ASIFSGLGVK VDLIDMRERL LSFLDDEISD ALSYHLRQNG VLVRHNEDYE
     SIEGDESGVI VKLKSGKRLR ADAFLWANGR TGNTDELGLE NIGLEPNGRG QLQVDEHYRT
     MVPHIYAVGD VIGWPSLASA AYDQGRSASD DFLDEDFRFV EDIPTGIYTI PEISSVGKNE
     RELTEAKVPY EVAQAFFKDT ARAQITGDTV GMLKILFHRE TLEILGIHCF GDQASEILHI
     GQAIMQQKGE ANTLKYFINT TFNYPTMAEA YRVAAQNGLN RVF
//