ID STHA_YERPN Reviewed; 466 AA.
AC Q1CNP4; D1Q371;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=YPN_0053; ORFNames=YP516_4591;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG16386.1; -; Genomic_DNA.
DR EMBL; ACNQ01000019; EEO74974.1; -; Genomic_DNA.
DR RefSeq; WP_002209477.1; NZ_ACNQ01000019.1.
DR AlphaFoldDB; Q1CNP4; -.
DR SMR; Q1CNP4; -.
DR GeneID; 66843486; -.
DR KEGG; ypn:YPN_0053; -.
DR HOGENOM; CLU_016755_0_0_6; -.
DR Proteomes; UP000008936; 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:0006739; P:NADP metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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_gammaproteobact.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR22912:SF93; SOLUBLE PYRIDINE NUCLEOTIDE TRANSHYDROGENASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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_0000260247"
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; 51382 MW; D6CD965D6CF3E2CE CRC64;
MQQHFHFDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYNN VGGGCTHWGT IPSKALRHAV
SRIIEFNQNP LYSDNARTIK SSFADILNHA DRVINQQTRM RQGFYDRNHC HMFSGDASFI
DANTVNVRYA DGTSDTLQAD NIVIATGSRP YRPVNVDFNH ERIYDSDTIL QLSHEPQHVI
IYGAGVIGCE YASIFRGLSV KVDLINTRDR LLAFLDQEMS DALSYHFWNN GVVIRHNEEF
EQIEGTTDGV IVHLKSGKKV KADCLLYANG RTGNTSGLGL ENIGLEADSR GLLKVNSMYQ
TALSHVYAVG DVIGYPSLAS AAYDQGRIAA QAMIKGEANV HLIEDIPTGI YTIPEISSVG
KTEQELTAMK VPYEVGRAQF KHLARAQIVG MDTGSLKILF HRETKQILGI HCFGERAAEI
IHIGQAIMEQ KGEGNTLEYF VNTTFNYPTM AEAYRVAALN GLNRLF
//
