ID   STHA_MYCBP              Reviewed;         468 AA.
AC   A1KM51;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=BCG_2726;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W.,
RA   Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C.,
RA   Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A.,
RA   Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(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.
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DR   EMBL; AM408590; CAL72714.1; -; Genomic_DNA.
DR   RefSeq; YP_978812.1; -.
DR   GeneID; 4698960; -.
DR   GenomeReviews; AM408590_GR; BCG_2726.
DR   KEGG; mbb:BCG_2726; -.
DR   OMA; A1KM51; 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    468       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_1000012559.
FT   NP_BIND      33     42       FAD (By similarity).
SQ   SEQUENCE   468 AA;  50754 MW;  D9E737C41C2898CF CRC64;
     MREYDIVVIG SGPGGQKAAI ASAKLGKSVA IVERGRMLGG VCVNTGTIPS KTLREAVLYL
     TGMNQRELYG ASYRVKDRIT PADLLARTQH VIGKEVDVVR NQLMRNRVDL IVGHGRFIDP
     HTILVEDQAR REKTTVTGDY IIIATGTRPA RPSGVEFDEE RVLDSDGILD LKSLPSSMVV
     VGAGVIGIEY ASMFAALGTK VTVVEKRDNM LDFCDPEVVE ALKFHLRDLA VTFRFGEEVT
     AVDVGSAGTV TTLASGKQIP AETVMYSAGR QGQTDHLDLH NAGLEVQGRG RIFVDDRFQT
     KVDHIYAVGD VIGFPALAAT SMEQGRLAAY HAFGEPTDGI TELQPIGIYS IPEVSYVGAT
     EVELTKSSIP YEVGVARYRE LARGQIAGDS YGMLKLLVST EDLKLLGVHI FGTSATEMVH
     IGQAVMGCGG SVEYLVDAVF NYPTFSEAYK NAALDVMNKM RALNQFRR
//