ID   STHA_ECOL6              Reviewed;         466 AA.
AC   Q8FB93;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 49.
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=c4923;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- SUBUNIT: Homooligomer; probable homooctamer (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; AE014075; AAN83351.1; -; Genomic_DNA.
DR   RefSeq; NP_756777.1; -.
DR   HSSP; P14218; 1LPF.
DR   GeneID; 1040055; -.
DR   GenomeReviews; AE014075_GR; c4923.
DR   KEGG; ecc:c4923; -.
DR   NMPDR; fig|199310.1.peg.4820; -.
DR   HOGENOM; Q8FB93; -.
DR   OMA; Q8FB93; GEGNTIE.
DR   BRENDA; 1.6.1.1; 292881.
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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    466       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000068062.
FT   NP_BIND      36     45       FAD (By similarity).
SQ   SEQUENCE   466 AA;  51573 MW;  AF61E5D1E2C582F2 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 QALVKGEANA HLIEDIPTGI YTIPEISSVG
     KTEQQLTAMK VPYEVGRAQF KHLARAQIVG MNVGTLKILF HRETKEILGI HCFGERAAEI
     IHIGQAIMEQ KGGGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF
//