ID   STHA_VIBVY              Reviewed;         466 AA.
AC   Q7MQ83;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-NOV-2008, entry version 35.
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=VV0126;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C.,
RA   Liao T.-L., Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L.,
RA   Shao C.-P., Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine
RT   pathogen.";
RL   Genome Res. 13:2577-2587(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; BA000037; BAC92889.1; -; Genomic_DNA.
DR   RefSeq; NP_932918.1; -.
DR   GeneID; 2622884; -.
DR   GenomeReviews; BA000037_GR; VV0126.
DR   KEGG; vvy:VV0126; -.
DR   HOGENOM; Q7MQ83; -.
DR   BioCyc; VVUL196600:VV0126-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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; IPR000759; Adrndx_reductase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
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; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   PRINTS; PR00411; PNDRDTASEI.
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_0000068078.
FT   NP_BIND      36     45       FAD (By similarity).
SQ   SEQUENCE   466 AA;  50955 MW;  A4DD36396FA20C01 CRC64;
     MAHANHFDVI VIGSGPGGEG AAMGLTKAGL KVAVVEKESS VGGGCTHWGT IPSKALRHAV
     SRIIEFNSNP LFCKNNSSLH ATFSTILGHA KSVIDKQTRL RQGFYDRNQC QLIFGTARFT
     DAHTISVTQN DGTEEVYTAD KFVIATGSRP YQPADVDFNH ERIYDSDSIL SLKHDPRHII
     IYGAGVIGCE YASIFRGLGV KTDLINTRDR LLAFLDNEVS DALSYHFWNS GVVIRNDETY
     ERIEGTEDGV IVHLQSGKKM KADCLLYANG RTGNTDKLNL PAVGLQGDSR GQLKVDGNYQ
     TEVEHVYAVG DVIGYPSLAS AAYDQGRFVA QAITKGKADG YLIDDIPTGI YTIPEISSVG
     KTEQELTAAK VPYEVGRSSF KHLARAQIAG KDIGSLKILF HRETKEILGI HCFGERAAEI
     IHIGQAIMEQ KGEANTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF
//