ID A0A160KU37_9MICO Unreviewed; 481 AA.
AC A0A160KU37;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:AND17079.1};
GN ORFNames=A6122_1954 {ECO:0000313|EMBL:AND17079.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND17079.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND17079.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND17079.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-2016) 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; CP015515; AND17079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160KU37; -.
DR STRING; 33888.A6122_1954; -.
DR KEGG; rtn:A6122_1954; -.
DR PATRIC; fig|33888.3.peg.2161; -.
DR Proteomes; UP000077071; Chromosome.
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:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 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:UP000077071}.
FT DOMAIN 13..345
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 366..473
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 202..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 481 AA; 50253 MW; E3A1C65F0ABFB0E6 CRC64;
MGLMAYEFER AQRIAVLGGG PGGYEAAIAG TQLGAEVTLV ERVGVGGSAV ITDVVPSKSL
IATAEATNAI GEAADLGVQF FTRSEQNKPV RPDVAVNLAT VNKRLLGLAR QQSEDMRANL
VHHGVRIVQG DGRLDGSTAL IVSTAAGGEG MDFDRIEADT IVVSVGASPR VLPTAAPDGE
RILSWTQLYT LKSVPEHLIV VGSGVTGAEF ASAYRALGAR VTLISSRDQV LPGEDADAAA
VIENVFKRNG MVVLSKSRAD RVERTEKGVQ AVLSDGRVVE GSHCLMAVGS VPNTAGIGLE
DAGVQLTESG HIRVNRVART SVPSIYAAGD CTTFLPLASV AAMQGRTGVF HAMGDAVNPT
EVRNVAANIF TQPEIATVGW SQREIEEGIA QGDIYKLPLA ANPRAKMMGI RDGFVKLFAR
TGSGTVIGGV IVAPKASELI FPLALAVEHR LTVDQVARAF TVYPSLTGSI SDAARAMHIV
S
//
