ID   STHA_SODGM              Reviewed;         465 AA.
AC   Q2NQZ3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=SG2157;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE75432.1; -; Genomic_DNA.
DR   RefSeq; YP_455837.1; -.
DR   GeneID; 3868266; -.
DR   GenomeReviews; AP008232_GR; SG2157.
DR   KEGG; sgl:SG2157; -.
DR   NMPDR; fig|343509.6.peg.4758; -.
DR   HOGENOM; Q2NQZ3; -.
DR   OMA; Q2NQZ3; GEGNTIE.
DR   BioCyc; SGLO343509:SG2157-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    465       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000260244.
FT   NP_BIND      36     45       FAD (By similarity).
SQ   SEQUENCE   465 AA;  51789 MW;  114D111ED8442D53 CRC64;
     MQPKYDYDAI IIGSGPGGEG AAMGLTKRGA RVAIIERYDN VGGGCTHWGT IPSKALRQAV
     SRIIEINQSP LHGNTRLPHT GFSDILCHAD QVINQQTHMR QGFYERNHCQ IFTGEASFVD
     EHQVQIHYGD NTTETLSAEN IVIACGSRPY QPQDVDFDHP RIYDSDSILD LKHDPHHVII
     YGAGVIGCEY ASIFRGMNVK VDLINTRDRL LAFLDQEMSD ALSYHFWENG VVIRHNEEYE
     EIKGLDDGVE VRFRSGKRMK ADCLLYANGR TGNTDTLKLD KVELEADSRG LIKVNSMYQT
     AARHIYAVGD VIGYPSLASA AYDQGRIAAQ VIIKGQANVQ LIENIPTGIY TIPEISSVGK
     TEQELTAMKV PYEVGRAQFK HLARAQIVGM NVGSLKLLFH RETKQILGIH CFGERAAEII
     HIGQAIMEQK GEGNTIEYFV NTTFNYPTMA EAYRVAALNG LNRLF
//