ID   STHA_HAHCH              Reviewed;         464 AA.
AC   Q2SIP2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=HCH_02695;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC29482.1; -; Genomic_DNA.
DR   RefSeq; YP_433907.1; -.
DR   GeneID; 3839006; -.
DR   GenomeReviews; CP000155_GR; HCH_02695.
DR   KEGG; hch:HCH_02695; -.
DR   NMPDR; fig|349521.5.peg.2402; -.
DR   HOGENOM; Q2SIP2; -.
DR   OMA; Q2SIP2; GEGNTIE.
DR   BioCyc; HCHE349521:HCH_02695-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    464       Soluble pyridine nucleotide
FT                                transhydrogenase.
FT                                /FTId=PRO_0000260236.
FT   NP_BIND      35     44       FAD (By similarity).
SQ   SEQUENCE   464 AA;  51435 MW;  1CEE8949202C5AD8 CRC64;
     MAEYRYDVVV IGAGPAGEGA AMNAAKHGKR VAVIEDKSQV GGNCTHMGTI PSKALRHAVK
     QIIQFNTNTM FRDIGEPRWF SFPRVLQNAE RVIGKQVKIR TQFYARNRVD LYRGRASFID
     ENRIEVRGGL NGKEVLYGKQ IVIATGSRPY LPEDVDFTHR RIYNSDSILK LSHTPRTLII
     YGAGVIGCEY ASIFVGLGVK VDLINPGERL LSFLDGEISD ALSYHLRDNG VLVRHNEQYD
     SVVGDDHGVV LTMKSGKRIR ADAFLWCNGR TGNTDNLGLE NIGLEPNARG QLAVDNHYRT
     KIPHVFAAGD VIGWPSLASA AYDQGRSASS EIVKDDFFRF ITDVPTGIYT IPEISSVGRT
     EAELTEAKVP YEVGQAFFKD LARAQITGDT VGMLKLLFHR ETMELLGIHC FGDQASEIVH
     IGQAIMNQPG ELNTIEYFVN TTFNYPTMAE AYRVAALNGL NRIF
//