ID   A0A0Q5AVH9_9MICO        Unreviewed;       480 AA.
AC   A0A0Q5AVH9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KQQ09630.1};
GN   ORFNames=ASF46_00355 {ECO:0000313|EMBL:KQQ09630.1};
OS   Rathayibacter sp. Leaf296.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ09630.1, ECO:0000313|Proteomes:UP000050868};
RN   [1] {ECO:0000313|EMBL:KQQ09630.1, ECO:0000313|Proteomes:UP000050868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ09630.1,
RC   ECO:0000313|Proteomes:UP000050868};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ09630.1, ECO:0000313|Proteomes:UP000050868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ09630.1,
RC   ECO:0000313|Proteomes:UP000050868};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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       ECO:0000256|RuleBase:RU003691}.
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:KQQ09630.1}.
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DR   EMBL; LMNR01000001; KQQ09630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5AVH9; -.
DR   STRING; 1736327.ASF46_00355; -.
DR   Proteomes; UP000050868; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 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.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050868}.
FT   DOMAIN          19..337
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          358..463
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         282
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         322
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        56..61
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   480 AA;  50883 MW;  57D0C370F4578F5E CRC64;
     MRGHPLDREA AVPDSIQHYD VAVIGAGPAG TAAALRAAEL GARVVVLEAA RVGGTCVNTG
     CVPTRVLAKT ARIIREARTA SDYGVDVGTP RIDWDATVRH VHERVDKVRS IKREAQRFEE
     AGVELIHEGR ARFADESTLV LDSGRRLTAS SILICVGGHS RRLPIPGAEL ATVPEDVLGL
     PSLPRRVAVI GGGNTGAQLV TVFNAFGSEV TLLDVAPRIL TTSDASISAY VAAAFERQGV
     RVSTGIETVE GIERADDALT LRWKDAGDSH AEQFDAVIMA TGWPADVEDL GLENAGIEVV
     RSAIPADQYF RTVVPHVFAV GDANGRDMLV QAAQFEAEAA AENAVLGANR RTPQHLLPAG
     GFTDPDYAGV GFTEEQARER DPQCVVASVP FSGVDRAVID DRESGFLTLI ADRRRELLLG
     AHAVGENAIE VVQSVTTAMA AGVDVATLAN VRFAYPTYSA VIGMAARALL KEPARPTELD
//