ID A0A1I2BC44_9PROT Unreviewed; 477 AA.
AC A0A1I2BC44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:SFE52873.1};
GN ORFNames=SAMN05428977_101936 {ECO:0000313|EMBL:SFE52873.1};
OS Nitrosomonas sp. Nm166.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=1881054 {ECO:0000313|EMBL:SFE52873.1, ECO:0000313|Proteomes:UP000199102};
RN [1] {ECO:0000313|EMBL:SFE52873.1, ECO:0000313|Proteomes:UP000199102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm166 {ECO:0000313|EMBL:SFE52873.1,
RC ECO:0000313|Proteomes:UP000199102};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FONE01000019; SFE52873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2BC44; -.
DR STRING; 1881054.SAMN05428977_101936; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000199102; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000199102}.
FT DOMAIN 10..323
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 346..449
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 143..145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 180..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 46..51
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 477 AA; 51644 MW; 3C1015738B232A25 CRC64;
MAEHTEETLD VIIIGAGSAG LSALREVRKR TKRFLIINDG PWGTTCARVG CMPSKLLIEA
ANAFHHRTTF DTFGIQGADQ LTIDITRVMQ RVRKLRDDFV ASTLATTQAL GARAISGRAR
ILGPNQVLVN DKNLDAKKII IATGSRPIVP VKWQALGNHL LTTDTLFEQE ELPASMAVVG
MGPIGVEMAQ ALSRLGIKVA GFGSNKLIGG LSDPRINQVA VDLLSQEFPL HLGEKAELIP
EPGKNCIFIQ AGDINVSVDK VLVALGRRPN IDDIGLETLG ISLNEQGLPP VNPETMQIAD
LPVFLAGDVN DHIPLLHEAA DEGHIAGLNA VRKEIVCFRR RTPLGIVFSD PTIATIGEHF
RLLNEKNIVI GEVNFDRQGR ARAAQRNKGV LRVYAESESG RLLGSEMCAP TGEHMAHLLA
LAIDRSLTVW DLLRLPYYHP VLEEGLRTAL RNLAAQLPAC SESDLASCGP FNADALD
//
