STHA_PSESM
ID STHA_PSESM Reviewed; 464 AA.
AC Q884I6;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
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=PSPTO_2106;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO55624.1; -; Genomic_DNA.
DR RefSeq; NP_791929.1; NC_004578.1.
DR RefSeq; WP_005771330.1; NC_004578.1.
DR AlphaFoldDB; Q884I6; -.
DR SMR; Q884I6; -.
DR STRING; 223283.PSPTO_2106; -.
DR EnsemblBacteria; AAO55624; AAO55624; PSPTO_2106.
DR GeneID; 1183753; -.
DR KEGG; pst:PSPTO_2106; -.
DR PATRIC; fig|223283.9.peg.2137; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_0_6; -.
DR OMA; CLMAVGA; -.
DR OrthoDB; 267896at2; -.
DR PhylomeDB; Q884I6; -.
DR Proteomes; UP000002515; 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; ISS:JCVI.
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;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..464
FT /note="Soluble pyridine nucleotide transhydrogenase"
FT /id="PRO_0000068071"
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; 50705 MW; EE89A8F997C129F7 CRC64;
MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDSRREV GGNCTHLGTI PSKALRHSVK
QIIQFNTNPM FRAIGEPRWF SFPDVLKNAE MVISKQVASR TSYYARNRVD VFFGTGSFAD
ETSVNVVCAN GVVEKLVANQ IIIATGSRPY RPADIDFSHK RIYDSDTILS LGHTPRKLII
YGAGVIGCEY ASIFSGLGVL VELVDNRDQL LSFLDSEISQ ALSYHFSNNN VMVRHNEEYE
RVEGLDNGVV LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NIGLKANGRG QIEVDEAYRT
SVSNVYGAGD VIGWPSLASA AYDQGRSAAG SMVDNGSWRY VNDVPTGIYT IPEISSIGKN
EHELTQAKVP YEVGKAFFKG MARAQISGER VGMLKILFHR ETLEVLGVHC FGDQASEIVH
IGQAIMSQPG EANTIKYFVN TTFNYPTMAE AYRVAAYDGL NRLF
