STHA_PSEPF
ID STHA_PSEPF Reviewed; 464 AA.
AC Q3K9F5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=Pfl01_3862;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA75599.1; -; Genomic_DNA.
DR RefSeq; WP_007953019.1; NC_007492.2.
DR AlphaFoldDB; Q3K9F5; -.
DR SMR; Q3K9F5; -.
DR STRING; 205922.Pfl01_3862; -.
DR PRIDE; Q3K9F5; -.
DR EnsemblBacteria; ABA75599; ABA75599; Pfl01_3862.
DR KEGG; pfo:Pfl01_3862; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_0_6; -.
DR OMA; CLMAVGA; -.
DR Proteomes; UP000002704; Chromosome.
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:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006739; P:NADP metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 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.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 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_0000260239"
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; 50891 MW; BB34A1B3B5826D16 CRC64;
MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRRQV GGNCTHLGTI PSKALRHSVR
QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVISKQVASR TGYYARNRVD VFFGTGSFAD
EQTIEVVCAN GVVEKLVAKH IIIATGSRPY RPADIDFHHP RIYDSDTILS LGHTPRKLIV
YGAGVIGCEY ASIFSGLGVL VELVDNRGQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYD
RVEGVDNGVI LHLKSGKKIK ADALLWCNGR TGNTDQLGLE NIGVKVNSRG QIEVDENYRT
CVQNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRF VNDVPTGIYT IPEISSIGKN
EQELTQAKVP YEVGKAFFKS MARAQIAGEP QGMLKILFHR ETLEVLGVHC FGYQASEIVH
IGQAIMNQPG ELNTLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF
