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Database: UniProt
Entry: E3C8J6_9LACO
LinkDB: E3C8J6_9LACO
Original site: E3C8J6_9LACO 
ID   E3C8J6_9LACO            Unreviewed;       445 AA.
AC   E3C8J6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFQ52969.1};
GN   ORFNames=HMPREF9265_0770 {ECO:0000313|EMBL:EFQ52969.1};
OS   Limosilactobacillus oris PB013-T2-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ52969.1, ECO:0000313|Proteomes:UP000003070};
RN   [1] {ECO:0000313|EMBL:EFQ52969.1, ECO:0000313|Proteomes:UP000003070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ52969.1,
RC   ECO:0000313|Proteomes:UP000003070};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:EFQ52969.1}.
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DR   EMBL; AEKL01000057; EFQ52969.1; -; Genomic_DNA.
DR   RefSeq; WP_003713153.1; NZ_AEKL01000057.1.
DR   AlphaFoldDB; E3C8J6; -.
DR   eggNOG; COG1249; Bacteria.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000003070; 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          7..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          332..439
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        430
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         165..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         255
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         296
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   445 AA;  48219 MW;  5CF636655B72C267 CRC64;
     MKTVQNIIIG FGKGGKTLAK FLAQQGEEVL VVEKSREMYG GTCINIACLP SKRLITEAAR
     GTDFATAIRG KREMVAQLRD KNYHMLADED TITVLDGTAH FTSDHTITVD TATGPQEFTG
     KRIFINTGAQ PTVPAIPGLQ ESPALLTSTS AMELDSLPQK LVIIGAGYIG LEFASMFAEF
     GAQVTVVDHH QEFLPREDAD VAAMVKANLE QAGVTFRLGV NINQVSTANG QTQVEISRDG
     HTTQLVADKI LAATGRRPAT AKLGLENTGI AVDDRGAIKV DDQLHTTVPG VWAIGDVKGG
     PQFTYISLDD FRIIKDELFG NGTRRISNRG VVPTSVFIEP PLAQVGLTEK QAHAQGQDYL
     LFKLPVAAIP KAKVLKDQRG VLKMLVDPQT KLILGATLYA PEAHEIINMV ALAMRAKLPY
     TLLRDQVYTH PTISEAFNDL LKKPQ
//
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