ID U4TL71_9LACO Unreviewed; 446 AA.
AC U4TL71;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glutathione reductase (NADPH) {ECO:0000313|EMBL:ERL65611.1};
GN ORFNames=L248_2297 {ECO:0000313|EMBL:ERL65611.1};
OS Schleiferilactobacillus shenzhenensis LY-73.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL65611.1, ECO:0000313|Proteomes:UP000030647};
RN [1] {ECO:0000313|Proteomes:UP000030647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX PubMed=24265500;
RA Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA Yang R., Liu F.;
RT "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL Genome Announc. 1:e00972-e00913(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; KI271585; ERL65611.1; -; Genomic_DNA.
DR RefSeq; WP_022528963.1; NZ_KI271585.1.
DR AlphaFoldDB; U4TL71; -.
DR STRING; 1231336.L248_2297; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_0_9; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000030647; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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 FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}.
FT DOMAIN 6..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 335..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 172..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 446 AA; 47118 MW; 6A4CA526E02126C5 CRC64;
MNTQHFDTLI IGGGPGGLAV AYGLAPHQHV AVVEADLWGG TCPNRGCDPK KMLYGAVASR
VQDQQYAGHG LIGAANVDWP ALMAFKRQYT EKVPSGTQKG LAANGVTTIH GAARLLDAHT
VSVARAEYTA DFIILATGAH AARPAIPGAE LLGTSTDFLD LDTLPRTMAF IGGGYVAVEL
ANIAANAGAE VHLIQHNHRL LRAFPETYTQ RLAQIMTDRG IIFHWDTSVT QVKETAAGVA
LTLSDGTPLT VAQAFSAIGR PANTNLDLAA VGITAKKGGI VVNDHLQTAQ PNIYAIGDVI
DKAAPKLTPV AGFEGRYVVS QILGTSTAAI RYPAVPHLVF ATPELGQVGV SVAAAQAAPD
QYTVTEQDLS GWYTYNRIQD RTARATVITD KQTHRLAGAV VLATDAEELL NYFALLIHQG
APASDLAQWI PVYPSVASDL SYLYQG
//
