ID   A0A3D8TVJ8_9LIST        Unreviewed;       445 AA.
AC   A0A3D8TVJ8;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:RDX03041.1};
GN   ORFNames=UR08_04050 {ECO:0000313|EMBL:RDX03041.1};
OS   Listeria kieliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1621700 {ECO:0000313|EMBL:RDX03041.1, ECO:0000313|Proteomes:UP000257055};
RN   [1] {ECO:0000313|Proteomes:UP000257055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kiel-L1 {ECO:0000313|Proteomes:UP000257055};
RA   Schardt J., Mueller-Herbst S., Scherer S., Huptas C.;
RL   Submitted (APR-2015) 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:RDX03041.1}.
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DR   EMBL; LARY01000001; RDX03041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8TVJ8; -.
DR   Proteomes; UP000257055; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257055}.
FT   DOMAIN          9..304
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          336..438
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         175..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         300
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        45..50
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   445 AA;  48738 MW;  8B192AE9FAC25D25 CRC64;
     MNNMDYKFDA IVIGSGVSGT SAAYALNEAG KKVAIIEERD WGGTCVLRGC DPKKVLAGAM
     EAHNFSERLR GKGIKQVAEI DWKDLQDFKK SFVESVPESR LEGFQEAKIE TFKGSAAFLD
     AHKLQVGEDT LSAEDIIIAT GARPNIPDIE GKEIFLTSDD FLDLETLPKR IAFVGGGYIA
     FEFAAIAHAA GSEVHLIHHN SRPLKGFDED HVAMLVSSLK SDGVHFHFDT DVEQLAKRDA
     GILLSAQNWT LEVDAVFATA GRKPNIERLN LEKAGIQSNR RGILVNQSLE AVPHVLAVGD
     VSVTPGLPLT PVDSFEADFA VSYILGKKQE IQYPAIPSAV FSSPKLAQVG LTAKEALQEK
     DRYHVNEIDM KNWYTYRRTN EYLSHAKVIT EKETGKIVGA SFISEEADVM INYIVLLMKA
     GLTLDALDSL IFAYPSPASD LPSLR
//