ID   A0A0R2MJL6_9LACO        Unreviewed;       444 AA.
AC   A0A0R2MJL6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Glutathione reductase {ECO:0000313|EMBL:KRO10986.1};
GN   ORFNames=IV64_GL002682 {ECO:0000313|EMBL:KRO10986.1};
OS   Lactiplantibacillus xiangfangensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO10986.1, ECO:0000313|Proteomes:UP000051783};
RN   [1] {ECO:0000313|EMBL:KRO10986.1, ECO:0000313|Proteomes:UP000051783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO10986.1,
RC   ECO:0000313|Proteomes:UP000051783};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRO10986.1}.
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DR   EMBL; JQCL01000057; KRO10986.1; -; Genomic_DNA.
DR   RefSeq; WP_057706484.1; NZ_JQCL01000057.1.
DR   AlphaFoldDB; A0A0R2MJL6; -.
DR   STRING; 942150.IV64_GL002682; -.
DR   PATRIC; fig|942150.3.peg.2794; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000051783; 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          5..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         299
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   444 AA;  47403 MW;  FCBD8CA17C57592E CRC64;
     MSTQYDVVVI GGGPAGTAVA SGLKAKGKNV LIVESDLWGG TCPNRGCDPK KILLSAVEAK
     VAAQNLQHTG LTGVPDVDWP ALMAHKRGYT DKINDGTLAG LKGQAIDTLH GEAFFQADGQ
     LTVDGTVIAT NDVVIATGQR PAILPVTGHE YFKTSTDFLD LDTMPKRVTF VGGGYVGFEL
     ATIANAAGAD VHLIHHNDRP LKEFDQTMVQ ALMANLTDAG VKFDLDQDLQ SITQEADGLH
     LKTATGFELV TDLVICSAGR VPNDDHLGLA HVGVQFGRHG IAVNDHLQTT NPHIYAVGDV
     SDTPIPKLTP VAGFEARYVV GQLTQPGAPI DYPVIPTQVY AAPKLAQVGL SAAEATAQPD
     RYVVNDLDMT TWFTYYRFSA KQALAKVVVD QTTGQAVGAT VLSDLADEMI NYLTLLIEQR
     LTVADLQRLV LAYPTPASDL QYLY
//