ID   STHA_ECO81              Reviewed;         466 AA.
AC   B7MR55;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
GN   Synonyms=udhA {ECO:0000255|HAMAP-Rule:MF_00247};
GN   OrderedLocusNames=ECED1_4669;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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; CU928162; CAR10639.1; -; Genomic_DNA.
DR   RefSeq; WP_001120819.1; NC_011745.1.
DR   AlphaFoldDB; B7MR55; -.
DR   SMR; B7MR55; -.
DR   PRIDE; B7MR55; -.
DR   EnsemblBacteria; CAR10639; CAR10639; ECED1_4669.
DR   KEGG; ecq:ECED1_4669; -.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   OMA; CLMAVGA; -.
DR   Proteomes; UP000000748; 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..466
FT                   /note="Soluble pyridine nucleotide transhydrogenase"
FT                   /id="PRO_1000193455"
FT   BINDING         36..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00247"
SQ   SEQUENCE   466 AA;  51572 MW;  6E0C54B9C0670AFD CRC64;
     MPHSYDYDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYQN VGGGCTHWGT IPSKALRHAV
     SRIIEFNQNP LYSDHSRLLR SSFADILNHA DNVINQQTRM RQGFYERNHC EILQGNARFV
     DEHTLALDCP DGSVETLTAE KFVIACGSRP YHPTDVDFTH PRIYDSNSIL SMHHEPRHVL
     IYGAGVIGCE YASIFRGMDV KVDLINTRDR LLAFLDQEMS DSLSYHFWNS GVVIRHNEEY
     EKIEGCDDGV IMHLKSGKKL KADCLLYANG RTGNTDSLAL QNIGLETDSR GQLKVNSMYQ
     TAQPHVYAVG DVIGYPSLAS AAYDQGRIAA QALVKGEANA HLIEDIPTGI YTIPEISSVG
     KTEQQLTAMK VPYEVGRAQF KHLARAQIVG MNVGTLKILF HRETKEILGI HCFGERAAEI
     IHIGQAIMEQ KGGGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF