ID   STHA_ECOK1              Reviewed;         466 AA.
AC   A1AIE2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Ecok1_39380;
GN   ORFNames=APECO1_2503;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ03432.1; -; Genomic_DNA.
DR   RefSeq; YP_859556.1; -.
DR   GeneID; 4491444; -.
DR   GenomeReviews; CP000468_GR; Ecok1_39380.
DR   KEGG; ecv:APECO1_2503; -.
DR   OMA; A1AIE2; GEGNTIE.
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    466       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_1000012556.
FT   NP_BIND      36     45       FAD (By similarity).
SQ   SEQUENCE   466 AA;  51560 MW;  2D7405D1E2D062FD CRC64;
     MPHSYDYDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYQN VGGGCTHWGT IPSKALRHAV
     SRIIEFNQNP LYSDHSRLLR SSFADILNHA DNVINQQTRM RQGFYERNHC EILQGNARFV
     DEHTLALDCP DGSVETLTAE KFVIACGSRP YHPTDVDFTH PRIYDSDSIL SMHHEPRHVL
     IYGAGVIGCE YASIFRGMDV KVDLINTRDR LLAFLDQEMS DSLSYHFWNS GVVIRHNEEY
     EKIEGCDDGV IMHLKSGKKL KADCLLYANG RTGNTDSLAL QNIGLETDSR GQLKVNSMYQ
     TAQPHVYAVG DVIGYPSLAS AAYDQGRIAA QALVKGEATA HLIEDIPTGI YTIPEISSVG
     KTEQQLTAMK VPYEVGRAQF KHLARAQIVG MNVGTLKILF HRETKEILGI HCFGERAAEI
     IHIGQAIMEQ KGGGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF
//