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Database: UniProt
Entry: G7LS46_9GAMM
LinkDB: G7LS46_9GAMM
Original site: G7LS46_9GAMM 
ID   G7LS46_9GAMM            Unreviewed;       468 AA.
AC   G7LS46;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=BrE312_4216 {ECO:0000313|EMBL:EHD23537.1};
OS   Brenneria sp. EniD312.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD23537.1};
RN   [1] {ECO:0000313|EMBL:EHD23537.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EniD312 {ECO:0000313|EMBL:EHD23537.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA   Glasner J., Perna N., Woyke T.;
RT   "Complete sequence of Brenneria sp. EniD312.";
RL   Submitted (JUL-2011) 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: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|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; CM001230; EHD23537.1; -; Genomic_DNA.
DR   RefSeq; WP_009114832.1; NZ_CM001230.1.
DR   AlphaFoldDB; G7LS46; -.
DR   STRING; 598467.BrE312_4216; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_0_6; -.
DR   Proteomes; UP000002759; 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 {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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00247}.
FT   DOMAIN          9..328
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          348..459
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         38..47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00247"
FT   BINDING         56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         185..192
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         272
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         313
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ   SEQUENCE   468 AA;  51571 MW;  46728C19FDD3B1E3 CRC64;
     MTLQQQFDYD AIVIGSGPGG EGAAMGLSKQ GAKIAVIERH YNVGGGCTHW GTIPSKALRH
     AVSRIIEFNQ NPLYSDNARI ISSSFSDILR HADSVIGQQT QMRQGFYERN QCELFSGEAR
     FIDAHTLAVH YPDNTHDTLT AANIIIASGS RPYHPAAVDF DHPRIYDSDS ILQLDHEPRH
     VIIYGAGVIG CEYASIFRGL NVKVDLINTR DRLLAFLDQE MSDALSYHFW NNGVVIRHNE
     EFESIEGVED GVIVNLKSGK KMKADCLLYA NGRTGNTETL GLEQIGLSTD SRGQLNVNSL
     YQTELAHIYA VGDVIGYPSL ASAAYDQGRL AAQAIIKGDA NAHLIEDIPT GIYTIPEISS
     VGKTEQQLTA MKVPYEVGRA QFKHLARAQI VGMNVGSLKI LFHRETKQIL GIHCFGERAA
     EIIHIGQAIM EQKGEGNTIE YFINTTFNYP TMAEAYRVAA LNGLNRLF
//
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