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Database: UniProt
Entry: A0A0A0B426_9CELL
LinkDB: A0A0A0B426_9CELL
Original site: A0A0A0B426_9CELL 
ID   A0A0A0B426_9CELL        Unreviewed;       477 AA.
AC   A0A0A0B426;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KGM00529.1};
GN   ORFNames=Q760_08210 {ECO:0000313|EMBL:KGM00529.1};
OS   Cellulomonas cellasea DSM 20118.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM00529.1, ECO:0000313|Proteomes:UP000029833};
RN   [1] {ECO:0000313|EMBL:KGM00529.1, ECO:0000313|Proteomes:UP000029833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM00529.1,
RC   ECO:0000313|Proteomes:UP000029833};
RA   Wang G., Zhuang W.;
RL   Submitted (OCT-2013) 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}.
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:KGM00529.1}.
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DR   EMBL; AXNT01000195; KGM00529.1; -; Genomic_DNA.
DR   RefSeq; WP_052104501.1; NZ_AXNT01000195.1.
DR   AlphaFoldDB; A0A0A0B426; -.
DR   STRING; 1408250.Q760_08210; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000029833; Unassembled WGS sequence.
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:UP000029833}.
FT   DOMAIN          5..325
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          347..451
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   477 AA;  49988 MW;  A658D27ABC647247 CRC64;
     MSDTYDVLVI GAGPAGTSAA LRAAELGARV AVVEARRTGG TCVNTGCVPT RVLAKTARLM
     REVRTADAYG ITVTEQTIDW PTTVARVRST VERVLAAKDE PDRLRAAGVD LVLEGRARFV
     GPHEVELEAS GRTLRAEQVI LCVGGHSRRL PVPGAELATL PEHVLDLPRL PRRVAVVGAG
     NTGAQLVTIF NAFGSDVTLL EVAPRILAQT DAAVSAAVAQ AFTEQGVRVV TSVEGVESLR
     QADDSSGIVL TWRAEGAEHR GTFDDVIMAT GWPASVEGLG LDAAGVQVER GRIVVDEYLR
     TSAAHVFAAG DANGQAMLVQ AAHVEAEAAA RNAVLGATRR TPHHLLPAGG FTDPDYAGVG
     LTEDQARARD RDCVVAHVAY DTMERPIIDD RPRGFLKLVA DRRRELLLGA HAVGENAVEV
     IQAVTTAMAA GVDVATLARV EFAYPTYSAV IGVAARQLLA VTPAEVLLAG AGARGSA
//
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