ID   STHA_MYCTU              Reviewed;         468 AA.
AC   P9WHH5; L0TAN4; O07212; P66006;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable soluble pyridine nucleotide transhydrogenase;
DE            Short=STH;
DE            EC=1.6.1.1;
DE   AltName: Full=NAD(P)(+) transhydrogenase [B-specific];
GN   Name=sthA; OrderedLocusNames=Rv2713; ORFNames=MTCY05A6.34;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Conversion of NADPH, generated by peripheral catabolic
CC       pathways, to NADH, which can enter the respiratory chain for energy
CC       generation. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45511.1; -; Genomic_DNA.
DR   PIR; D70532; D70532.
DR   RefSeq; NP_217229.1; NC_000962.3.
DR   RefSeq; WP_003900556.1; NZ_NVQJ01000017.1.
DR   AlphaFoldDB; P9WHH5; -.
DR   SMR; P9WHH5; -.
DR   STRING; 83332.Rv2713; -.
DR   PaxDb; P9WHH5; -.
DR   DNASU; 887355; -.
DR   GeneID; 45426700; -.
DR   GeneID; 887355; -.
DR   KEGG; mtu:Rv2713; -.
DR   PATRIC; fig|83332.111.peg.3018; -.
DR   TubercuList; Rv2713; -.
DR   eggNOG; COG1249; Bacteria.
DR   OMA; SGHAAWH; -.
DR   PhylomeDB; P9WHH5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..468
FT                   /note="Probable soluble pyridine nucleotide
FT                   transhydrogenase"
FT                   /id="PRO_0000068065"
FT   BINDING         33..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  50754 MW;  D9E737C41C2898CF CRC64;
     MREYDIVVIG SGPGGQKAAI ASAKLGKSVA IVERGRMLGG VCVNTGTIPS KTLREAVLYL
     TGMNQRELYG ASYRVKDRIT PADLLARTQH VIGKEVDVVR NQLMRNRVDL IVGHGRFIDP
     HTILVEDQAR REKTTVTGDY IIIATGTRPA RPSGVEFDEE RVLDSDGILD LKSLPSSMVV
     VGAGVIGIEY ASMFAALGTK VTVVEKRDNM LDFCDPEVVE ALKFHLRDLA VTFRFGEEVT
     AVDVGSAGTV TTLASGKQIP AETVMYSAGR QGQTDHLDLH NAGLEVQGRG RIFVDDRFQT
     KVDHIYAVGD VIGFPALAAT SMEQGRLAAY HAFGEPTDGI TELQPIGIYS IPEVSYVGAT
     EVELTKSSIP YEVGVARYRE LARGQIAGDS YGMLKLLVST EDLKLLGVHI FGTSATEMVH
     IGQAVMGCGG SVEYLVDAVF NYPTFSEAYK NAALDVMNKM RALNQFRR