ID L8TY56_9MICC Unreviewed; 471 AA.
AC L8TY56;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:ELT46189.1};
DE SubName: Full=NAD(P)H-quinone dehydrogenase {ECO:0000313|EMBL:TDL36387.1};
GN ORFNames=E2R57_14280 {ECO:0000313|EMBL:TDL36387.1}, G205_00500
GN {ECO:0000313|EMBL:ELT46189.1};
OS Arthrobacter nitrophenolicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT46189.1, ECO:0000313|Proteomes:UP000011189};
RN [1] {ECO:0000313|EMBL:ELT46189.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|EMBL:ELT46189.1};
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.S.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:E00058-13(2013).
RN [2] {ECO:0000313|Proteomes:UP000011189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:e0005813-e0005813(2013).
RN [3] {ECO:0000313|EMBL:TDL36387.1, ECO:0000313|Proteomes:UP000294621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-A1 {ECO:0000313|EMBL:TDL36387.1,
RC ECO:0000313|Proteomes:UP000294621};
RA Steinbock B., Bechtold R., Sevigny J.L., Thomas D., Cuthill L.R.,
RA Aveiro Johannsen E.J., Thomas K., Ghosh A.;
RT "Genome Sequencing and Assembly of Various Microbes Isolated from Partially
RT Reclaimed Soil and Acid Mine Drainage (AMD) Site.";
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}.
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:ELT46189.1}.
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DR EMBL; AOFD01000001; ELT46189.1; -; Genomic_DNA.
DR EMBL; SMZQ01000007; TDL36387.1; -; Genomic_DNA.
DR RefSeq; WP_009356279.1; NZ_SMZQ01000007.1.
DR AlphaFoldDB; L8TY56; -.
DR STRING; 683150.G205_00500; -.
DR PATRIC; fig|683150.5.peg.101; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000011189; Unassembled WGS sequence.
DR Proteomes; UP000294621; 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:UP000011189}.
FT DOMAIN 11..335
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 356..463
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 127
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 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 471 AA; 49288 MW; A120E89933D7CCD5 CRC64;
MTTHPDFSSP RIAILGGGPG GYEAAMVAAS LGAQVTIIER AGLGGSAVLT DVVPSKTLIA
TADLMTRVAE AGELGVKFDV DGGDFVPVMR ADLKHINDRL LNLARSQSKD IHDGLEGQGV
RILTGSGRLL DNHTIEVITL DGTEIVEADT ILLAVGAHPR ELPTARPDGE RILNWTQIYN
LDELPEDLIV VGSGVTGAEF ASAYNGLGSK VTLVSSRDRV LPGSDVDAAV VLEEVFERRG
VRVMSRSRAE SVERTEDGVV VTLSDGSKVT GSHCLLCLGS IPNTAGIGLE EAGVALSESG
HIKVDGVSRT SAPNIYAAGD CTGVLPLASV AAMQGRIAVA HFMGDVVTPL KLHQVASNIF
TSPEIANVGV SEAEIESGKY QGDVVKLSLR SNARAKMRNA RDGFVKIFAR KGSGTVIGGV
VVGPNASELI FPISIAVKQK LHVDDVASTF TVYPSLTGSI SEAARRLHVH L
//
