ID A0A0C5BUY5_9MICO Unreviewed; 475 AA.
AC A0A0C5BUY5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:KKM47375.1};
DE SubName: Full=NAD(P)H-quinone dehydrogenase {ECO:0000313|EMBL:PPI14025.1};
GN ORFNames=C5C51_08750 {ECO:0000313|EMBL:PPI14025.1}, VT73_00235
GN {ECO:0000313|EMBL:KKM47375.1};
OS Rathayibacter toxicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM47375.1, ECO:0000313|Proteomes:UP000052979};
RN [1] {ECO:0000313|EMBL:KKM47375.1, ECO:0000313|Proteomes:UP000052979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH142 {ECO:0000313|EMBL:KKM47375.1,
RC ECO:0000313|Proteomes:UP000052979};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA 70134 or
RT CS 32), a Western Australian isolate.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPI14025.1, ECO:0000313|Proteomes:UP000237966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH99 {ECO:0000313|EMBL:PPI14025.1,
RC ECO:0000313|Proteomes:UP000237966};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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:KKM47375.1}.
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DR EMBL; LBFI01000001; KKM47375.1; -; Genomic_DNA.
DR EMBL; PSWU01000013; PPI14025.1; -; Genomic_DNA.
DR RefSeq; WP_027691756.1; NZ_PSXN01000014.1.
DR AlphaFoldDB; A0A0C5BUY5; -.
DR STRING; 145458.APU90_08125; -.
DR GeneID; 66873639; -.
DR KEGG; rtc:APU90_08125; -.
DR KEGG; rtx:TI83_08950; -.
DR PATRIC; fig|145458.7.peg.2041; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000052979; Unassembled WGS sequence.
DR Proteomes; UP000237966; 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: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:UP000052979}.
FT DOMAIN 10..339
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 361..467
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 196..203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 324
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 475 AA; 49420 MW; 62AAE0148A066243 CRC64;
MADEFERVQR IAVLGGGPGG YEAAIAGAQL GAEVTLVEQV GVGGSAVLTD VVPSKSLIAT
AEAASAIGEA ADLGVQFFTR SDRNTPVSPE IAVNLATVNT RLLGLAGQQS EDLRANLVHH
GVRIVPGRGR LDGANALMVS TADGRDGDRI EADTIVVSVG ASPRVLSSAV PDGERILNWT
QLYTLPAVPE HLIVVGSGVT GVEFASAYRA LGARVTLISS RDRVLPGEDE DAAAVIENVF
TRNGMVVLSQ SRATRVELTK TGVRAVLSDG RMVEGSHCLM AVGSVPNTVG IGLEEAGVQL
SESGHIRVNR VARTSMPSIY AAGDCTNFLP LASVAAMQGR TAAFHAMGDV VNPTEVRNVS
ANIFTQPEIA TVGWSQREIE EGLAQGEVCT LPLSANARAK MMGIRDGFVK LFARTGSGTV
IGGVIVAPKA SELIFPLALA VENRLTVDNV ARAFTVYPSL TGSLSEAARA MHIVV
//
