STHA_ECOLI
ID STHA_ECOLI Reviewed; 466 AA.
AC P27306; Q2M8Q7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Soluble pyridine nucleotide transhydrogenase;
DE Short=STH;
DE EC=1.6.1.1 {ECO:0000269|PubMed:9922271};
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific];
GN Name=sthA; Synonyms=sth, udhA; OrderedLocusNames=b3962, JW5551;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=9922271; DOI=10.1128/jb.181.3.1030-1034.1999;
RA Boonstra B., French C.E., Wainwright I., Bruce N.C.;
RT "The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide
RT transhydrogenase.";
RL J. Bacteriol. 181:1030-1034(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.
RC STRAIN=K12;
RX PubMed=1447162; DOI=10.1128/jb.174.23.7878-7879.1992;
RA Gustafsson C., Warne S.R.;
RT "Physical map of the oxyR-trmA region (minute 89.3) of the Escherichia coli
RT chromosome.";
RL J. Bacteriol. 174:7878-7879(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 347-466.
RX PubMed=2511419; DOI=10.1007/bf00332397;
RA Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.;
RT "Molecular cloning and nucleotide sequencing of oxyR, the positive
RT regulatory gene of a regulon for an adaptive response to oxidative stress
RT in Escherichia coli: homologies between OxyR protein and a family of
RT bacterial activator proteins.";
RL Mol. Gen. Genet. 218:371-376(1989).
CC -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC pathways, to NADH, which can enter the respiratory chain for energy
CC generation. {ECO:0000269|PubMed:9922271}.
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:0000269|PubMed:9922271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11693;
CC Evidence={ECO:0000269|PubMed:9922271};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9922271};
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Homooligomer; probable homooctamer.
CC {ECO:0000269|PubMed:9922271}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43068.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA46822.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00006; AAC43068.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76944.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77349.1; -; Genomic_DNA.
DR EMBL; X66026; CAA46822.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X16531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E65203; E65203.
DR RefSeq; NP_418397.2; NC_000913.3.
DR RefSeq; WP_001120810.1; NZ_STEB01000037.1.
DR AlphaFoldDB; P27306; -.
DR SMR; P27306; -.
DR BioGRID; 4263449; 8.
DR BioGRID; 852757; 1.
DR IntAct; P27306; 1.
DR STRING; 511145.b3962; -.
DR jPOST; P27306; -.
DR PaxDb; P27306; -.
DR PRIDE; P27306; -.
DR EnsemblBacteria; AAC76944; AAC76944; b3962.
DR EnsemblBacteria; BAE77349; BAE77349; BAE77349.
DR GeneID; 66672126; -.
DR GeneID; 948461; -.
DR KEGG; ecj:JW5551; -.
DR KEGG; eco:b3962; -.
DR PATRIC; fig|1411691.4.peg.2743; -.
DR EchoBASE; EB1398; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_0_6; -.
DR InParanoid; P27306; -.
DR OMA; CLMAVGA; -.
DR PhylomeDB; P27306; -.
DR BioCyc; EcoCyc:UDHA-MON; -.
DR BioCyc; MetaCyc:UDHA-MON; -.
DR BRENDA; 1.6.1.1; 2026.
DR PRO; PR:P27306; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IDA:EcoCyc.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9922271"
FT CHAIN 2..466
FT /note="Soluble pyridine nucleotide transhydrogenase"
FT /id="PRO_0000068061"
FT BINDING 36..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CONFLICT 64
FT /note="I -> L (in Ref. 5; CAA46822)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="R -> L (in Ref. 5; CAA46822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51560 MW; 2D7405D1E2D062FD CRC64;
MPHSYDYDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYQN VGGGCTHWGT IPSKALRHAV
SRIIEFNQNP LYSDHSRLLR SSFADILNHA DNVINQQTRM RQGFYERNHC EILQGNARFV
DEHTLALDCP DGSVETLTAE KFVIACGSRP YHPTDVDFTH PRIYDSDSIL SMHHEPRHVL
IYGAGVIGCE YASIFRGMDV KVDLINTRDR LLAFLDQEMS DSLSYHFWNS GVVIRHNEEY
EKIEGCDDGV IMHLKSGKKL KADCLLYANG RTGNTDSLAL QNIGLETDSR GQLKVNSMYQ
TAQPHVYAVG DVIGYPSLAS AAYDQGRIAA QALVKGEATA HLIEDIPTGI YTIPEISSVG
KTEQQLTAMK VPYEVGRAQF KHLARAQIVG MNVGTLKILF HRETKEILGI HCFGERAAEI
IHIGQAIMEQ KGGGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF
