ID   STHA_COLP3              Reviewed;         466 AA.
AC   Q48A14;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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; OrderedLocusNames=CPS_0334;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ24633.1; -; Genomic_DNA.
DR   RefSeq; YP_267100.1; -.
DR   GeneID; 3518988; -.
DR   GenomeReviews; CP000083_GR; CPS_0334.
DR   KEGG; cps:CPS_0334; -.
DR   NMPDR; fig|167879.3.peg.192; -.
DR   TIGR; CPS_0334; -.
DR   HOGENOM; Q48A14; -.
DR   OMA; Q48A14; GEGNTIE.
DR   BioCyc; CPSY167879:CPS_0334-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    466       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000260232.
FT   NP_BIND      36     45       FAD (By similarity).
SQ   SEQUENCE   466 AA;  51181 MW;  F82A52806BF28019 CRC64;
     MEKSFDYDVI IIGTGPGGEG AAMNLAKRQK KVAIIERYHQ VGGGCTHWGT IPSKALRQSV
     SRLIEYNSNP LFNQNEQVKQ LTFQDILSHA SAVIQKQVSL RSGFYNRNRV EHIQGQASFI
     DAHTISISHP DGSVEKISAK QIMIATGSRP YRPDDIDFDH PRVYDSDSIL SLKHAPQHVI
     IYGAGVIGSE YASIFRGLGV KVDLINTRER LLSFLDTEMS DSLSYHLWNS GVVIRHGEEI
     ERVESSEDAV IVHLKSGKKM RADCLLFANG RTGNTADLNL AAAGLKADGR GQLKVNDCYQ
     TEVDNIFAVG DVIGYPSLAS AAFDQGRIAA SAMVDSSSKA KLIVDIPTGI YTIPEISSVG
     KTEQELTEAK IPYEVGRAQF KHLARAQISN NLVGSLKILF HRETKEILGI HCFGENAAEI
     IHIGQAIMQQ TNGGNTIEYF VETTFNYPTM AEAFRVAALN GLNRLF
//