ID A0A1D8T8P9_9NOCA Unreviewed; 491 AA.
AC A0A1D8T8P9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AOW93966.1};
GN ORFNames=BFN03_18410 {ECO:0000313|EMBL:AOW93966.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW93966.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW93966.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW93966.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-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,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CP017014; AOW93966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8T8P9; -.
DR STRING; 679318.BFN03_18410; -.
DR KEGG; rhw:BFN03_18410; -.
DR Proteomes; UP000178767; Chromosome.
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:UP000178767}.
FT DOMAIN 22..331
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 351..454
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 192..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 58..63
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 491 AA; 51279 MW; 303FE0575E0689A6 CRC64;
MTQKEFQNVA PASRKSFPGS ADLVVIGGGA AGIVAAKTAA GFGAKVVLVE RDRTGGDCLW
TGCVPSKALL AAASVAATMR RGHEFGVDAS NVTVDFARVM KHVQGAIETI APVDSPETLR
DANVNVVSGT ARFTGPRSLS IDSHTITFGQ AVIATGAAPA VPNIHGLDQV DYLTSDTIWG
LTELPPRLLV LGGGSVGCEL AQAFARLGST VTIVEAADSL LPAEDREAAA FVTQSLVDDG
VTVLTGVTAE SVAGQALVLA DGRHLEFDSL LVAVGRKPRT ASIGLDAAGV TVDRRGFVTV
DDHLRTTNPR VWAAGDLTGH PQFTHTAGMH GSIAATNAIL GLRRTVDRTG TPRVTFTDPE
IAVAGIDTEA ARRIPGLHVH TLGHEHVDRA VAERETRGFT RLVVDGKHRI VGATVVGPRA
GETIGEIVLA IKQGLRTRDL AGTTHPYPTY NDGPWNASIA DVRSQLAKPV ASGAIKVLAR
IRRAAQNIRK D
//
