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Database: UniProt
Entry: Q82WB8_NITEU
LinkDB: Q82WB8_NITEU
Original site: Q82WB8_NITEU 
ID   Q82WB8_NITEU            Unreviewed;       472 AA.
AC   Q82WB8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase, class I {ECO:0000313|EMBL:CAD84685.1};
DE            EC=1.8.1.4 {ECO:0000313|EMBL:CAD84685.1};
GN   OrderedLocusNames=NE0774 {ECO:0000313|EMBL:CAD84685.1};
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD84685.1, ECO:0000313|Proteomes:UP000001416};
RN   [1] {ECO:0000313|EMBL:CAD84685.1, ECO:0000313|Proteomes:UP000001416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC   {ECO:0000313|Proteomes:UP000001416};
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA   Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA   Whittaker M., Arp D.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84685.1; -; Genomic_DNA.
DR   RefSeq; WP_011111386.1; NC_004757.1.
DR   AlphaFoldDB; Q82WB8; -.
DR   STRING; 228410.NE0774; -.
DR   KEGG; neu:NE0774; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_3_4; -.
DR   OrthoDB; 178496at2; -.
DR   PhylomeDB; Q82WB8; -.
DR   Proteomes; UP000001416; Chromosome.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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   Oxidoreductase {ECO:0000313|EMBL:CAD84685.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001416}.
FT   DOMAIN          4..316
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          340..444
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        434
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         138..140
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         175..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        41..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   472 AA;  51148 MW;  7E1A210945561893 CRC64;
     MHKFDVVIIG AGSAGLSALR EVKKHTDNFI LINEGPWGTT CARVGCMPSK LLIEAANAFY
     RRVSFNEFGI TGADQLGVDH KRVLQRVRRL RDDFVTSTLG ATRELGERAI SGRAHILSPH
     QVMVNGEKFH TRKIIIATGS RPVVPEPWQS LGKRLFTTDT LFEQEALPER IAVIGMGPVG
     LEMAQALSRL GVRVTGFGSG RMIGGITDPL INQAAVTLLS KEFSLHLGTR ADITVNVDSD
     VITVNSGDIR IEVDSVLAAL GRRPNIDDIN LEALGVPLDE RGLPPVNPDT LQIADLPVFL
     AGDVNQRSPV LHEAADDGHI AGLNATREKL VCFKRRVPLT IVFSDPNIAV VGKSFRSLEH
     EDIRAGEVDF SRQGRARSAQ SNRGVLRVYA AANSGRLLGA EMCAPAGEHF AHLLALAIDQ
     SLSVWDLLRL PFYHPVLEEG LRTALRNLAS KLPACSESDL AVCGPFNAEA LD
//
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