ID   STHA_PHOLL              Reviewed;         465 AA.
AC   Q7MBG9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=udhA; OrderedLocusNames=plu4739;
OS   Photorhabdus luminescens subsp. laumondii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=141679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TT01;
RX   MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S.,
RA   Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V.,
RA   Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571874; CAE17111.1; -; Genomic_DNA.
DR   RefSeq; NP_931901.1; -.
DR   GeneID; 2804786; -.
DR   GenomeReviews; BX470251_GR; plu4739.
DR   KEGG; plu:plu4739; -.
DR   NMPDR; fig|243265.1.peg.4524; -.
DR   PhotoList; plu4739; -.
DR   HOGENOM; Q7MBG9; -.
DR   OMA; Q7MBG9; GEGNTIE.
DR   BioCyc; PLUM243265:PLU4739-MON; -.
DR   BRENDA; 1.6.1.1; 308689.
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    465       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000068067.
FT   NP_BIND      35     44       FAD (By similarity).
SQ   SEQUENCE   465 AA;  51482 MW;  782044DE12946CCE CRC64;
     MQHIHFDAIV IGSGPGGEGA AMGLVKQGKS VAVIERYNNV GGGCTHWGTI PSKALRHAVS
     RIIEFNQNPL YSDNSRVLRS SFAEILRRAE MVINQQTRMR QGFYERNGCR MFSGEATFID
     DHRVSVRYAD DNHDILSADK IIIATGSRPY CPPDVDFTHS RIYNSDSILK LDHEPRHVII
     YGAGVIGCEY ASIFRGLGVK VDLINTRNHL LAFLDQEMSD ALSYHFWNSG IVIRHNEEYS
     KIEGVDDGVI VHLKSGKKVK ADCLLYANGR TGNTDTLGLK NVGLEADSRG LLKVNKIYQT
     SNENIYAVGD VIGYPSLASA AYDQGRIAAQ AMTKGNAEVH LIEDIPTGIY TIPEISSVGK
     TEQQLTAMKV PYEVGRAQFK HLARAQIAGM NVGSLKILFH RETKEILGIH CFGERAAEII
     HIGQAIMEQK GESNTIEYFV NTTFNYPTMA EAYRVAALNG LNRLF
//