ID STHA_PSEP1 Reviewed; 464 AA.
AC A5W6F5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000255|HAMAP-Rule:MF_00247};
DE Short=STH {ECO:0000255|HAMAP-Rule:MF_00247};
DE EC=1.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00247};
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000255|HAMAP-Rule:MF_00247};
GN Name=sthA {ECO:0000255|HAMAP-Rule:MF_00247}; OrderedLocusNames=Pput_3591;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC pathways, to NADH, which can enter the respiratory chain for energy
CC generation. {ECO:0000255|HAMAP-Rule:MF_00247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + NADPH = NADH + NADP(+); Xref=Rhea:RHEA:11692,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58349; EC=1.6.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00247};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00247};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00247};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00247}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000255|HAMAP-Rule:MF_00247}.
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DR EMBL; CP000712; ABQ79715.1; -; Genomic_DNA.
DR AlphaFoldDB; A5W6F5; -.
DR SMR; A5W6F5; -.
DR KEGG; ppf:Pput_3591; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_0_6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006739; P:NADP metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR HAMAP; MF_00247; SthA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR022962; STH_gammaproteobact.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR22912:SF93; SOLUBLE PYRIDINE NUCLEOTIDE TRANSHYDROGENASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase.
FT CHAIN 1..464
FT /note="Soluble pyridine nucleotide transhydrogenase"
FT /id="PRO_1000012565"
FT BINDING 35..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00247"
SQ SEQUENCE 464 AA; 50906 MW; 6A86683818494616 CRC64;
MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDDRRQV GGNCTHLGTI PSKALRHSVR
QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVIAKQVASR TGYYARNRVD VFVGTGSFAD
EQTVEVVCPN GVVEKLNAKH IIIATGSRPY RPADIDFHHP RVYDSDTILS LSHTPRKLIV
YGAGVIGCEY ASIFSGLGVL VELVDNRGQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYE
RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NIGIKVNSRG QIEVDEAYRT
TVPNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRF VNDVPTGIYT IPEISSIGKN
EQELTQAKVP YEVGKAFFKS MARAQIAGEP QGMLKILFHR ETLEILGVHC FGYQASEIVH
IGQAIMNQPG EQNNLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF
//
