ID F4N170_YEREN Unreviewed; 466 AA.
AC F4N170;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Soluble pyridine nucleotide transhydrogenase {ECO:0000256|ARBA:ARBA00016603, ECO:0000256|HAMAP-Rule:MF_00247};
DE Short=STH {ECO:0000256|HAMAP-Rule:MF_00247};
DE EC=1.6.1.1 {ECO:0000256|ARBA:ARBA00012772, ECO:0000256|HAMAP-Rule:MF_00247};
DE AltName: Full=NAD(P)(+) transhydrogenase [B-specific] {ECO:0000256|ARBA:ARBA00031183, ECO:0000256|HAMAP-Rule:MF_00247};
GN Name=sthA {ECO:0000256|HAMAP-Rule:MF_00247};
GN ORFNames=YEW_AP03080 {ECO:0000313|EMBL:CBX71828.1};
OS Yersinia enterocolitica W22703.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=913028 {ECO:0000313|EMBL:CBX71828.1};
RN [1] {ECO:0000313|EMBL:CBX71828.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21453472; DOI=10.1186/1471-2164-12-168;
RA Fuchs T.M., Brandt K., Starke M., Rattei T.;
RT "Shotgun sequencing of Yersinia enterocolitica strain W22703 (biotype 2,
RT serotype O:9): genomic evidence for oscillation between invertebrates and
RT mammals.";
RL BMC Genomics 12:168-168(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:0000256|ARBA:ARBA00002842, ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-
CC Rule:MF_00247};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00247,
CC ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_00247,
CC ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00247}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|HAMAP-Rule:MF_00247}.
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DR EMBL; FR718673; CBX71828.1; -; Genomic_DNA.
DR AlphaFoldDB; F4N170; -.
DR SMR; F4N170; -.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00247};
KW FAD {ECO:0000256|HAMAP-Rule:MF_00247, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00247};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00247};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00247};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00247,
KW ECO:0000313|EMBL:CBX71828.1}.
FT DOMAIN 8..326
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 346..457
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 36..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00247"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 146..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 183..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 466 AA; 51376 MW; C3A5AC35262BCFC5 CRC64;
MQQHFHFDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYNN VGGGCTHWGT IPSKALRHAV
SRIIEFNQNP LYSDNARTIS SSFSDILNHA DRVINQQTRM RQGFYDRNHC QMFSGDASFI
DANTINVRYA DGTNDTLRAD NIVIATGSRP YRPANVDFTH ERIYDSDTIL QLSHEPQHVI
IYGAGVIGCE YASIFRGLSV KVDLINTRDR LLAFLDQEMS DALSYHFWNN GVVIRHNEEF
EQIEGTVDGV IVHLKSGKKV KADCLLYANG RTGNTSGLGL EKIGLEADSR GLLKVNSMYQ
TALSHVYAVG DVIGYPSLAS AAYDQGRIAA QAMIKGEANT HLIEDIPTGI YTIPEISSVG
KTEQDLTAMK VPYEVGRAQF KHLARAQIVG MDTGSLKILF HRETKQILGI HCFGERAAEI
IHIGQAIMEQ KGEGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF
//
