ID A0A2S0WJ45_9ACTN Unreviewed; 446 AA.
AC A0A2S0WJ45; A0A5F2ERK7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:TGN30708.1};
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AWB91359.1};
GN ORFNames=C3E78_03500 {ECO:0000313|EMBL:AWB91359.1}, E4L97_16635
GN {ECO:0000313|EMBL:TGN30708.1};
OS Aeromicrobium chenweiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2079793 {ECO:0000313|EMBL:AWB91359.1, ECO:0000313|Proteomes:UP000244384};
RN [1] {ECO:0000313|EMBL:AWB91359.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=592 {ECO:0000313|EMBL:AWB91359.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000244384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=592 {ECO:0000313|Proteomes:UP000244384};
RA Li J.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TGN30708.1, ECO:0000313|Proteomes:UP000297606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S592 {ECO:0000313|EMBL:TGN30708.1,
RC ECO:0000313|Proteomes:UP000297606};
RA Li J., Ha Z., Lu H., Jin N.;
RL Submitted (MAR-2019) 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}.
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DR EMBL; CP026952; AWB91359.1; -; Genomic_DNA.
DR EMBL; SRPI01000009; TGN30708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WJ45; -.
DR KEGG; aez:C3E78_03500; -.
DR OrthoDB; 4763248at2; -.
DR Proteomes; UP000244384; Chromosome.
DR Proteomes; UP000297606; 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..316
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..444
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 178..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 302
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 446 AA; 46513 MW; E87083D061E0B3D2 CRC64;
MTEISCDVVV VGTGPGGEAL VPRLAKAGLD VVAVEAELVG GECPYWGCIP SKMVIRAANA
LAEARRAEQL AGSVSVAPDF SFVAKRIREE ATANWDDTVA ADRITAAGAR LVRGRGRLDG
ERRVTVGDDT YVASKGVVLN TGTTTFVPPI DGLAGTPFWT NREILEAEEA PASLIVIGGG
AVGLEMAQAF ARFGTAVTVL EVGPRVLAVE EPESSELVAS VFEAEGIGIH AGITIDGVAH
DGEVFHVTSG GVTYEAERVL VAAGRRSRVD DIGLDTVGVE AGRFLTVDDS MQVTDGLWAI
GDMVGRGAFT HVSMYQSARA AKAVLGEDLP EYDDSLPRVT FTDPEIGAVG ITEAQARERG
INVRIGSTDV AASSRGFVHG PGNQGFIKLV IDDDRGVIVG ATSAGPYGGE TLSALAFAVR
AEIPVATLVN TVYAYPTFWR AIESAL
//
