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Entry: S5MM98_SALBN
LinkDB: S5MM98_SALBN
Original site: S5MM98_SALBN 
ID   S5MM98_SALBN            Unreviewed;       441 AA.
AC   S5MM98;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Putative Dihydrolipoamide dehydrogenase-disulfide oxidoreductase {ECO:0000313|EMBL:AGR57721.1};
GN   ORFNames=A464_535 {ECO:0000313|EMBL:AGR57721.1};
OS   Salmonella bongori N268-08.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1197719 {ECO:0000313|EMBL:AGR57721.1, ECO:0000313|Proteomes:UP000015042};
RN   [1] {ECO:0000313|EMBL:AGR57721.1, ECO:0000313|Proteomes:UP000015042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N268-08 {ECO:0000313|EMBL:AGR57721.1,
RC   ECO:0000313|Proteomes:UP000015042};
RA   Marti R., Hagens S., Loessner M.J., Klumpp J.;
RT   "Genome sequence of Salmonella bongori N268-08 - a rare clinical isolate.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP006608; AGR57721.1; -; Genomic_DNA.
DR   RefSeq; WP_000195938.1; NC_021870.1.
DR   AlphaFoldDB; S5MM98; -.
DR   GeneID; 66755031; -.
DR   KEGG; sbz:A464_535; -.
DR   PATRIC; fig|1197719.3.peg.534; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_1_2_6; -.
DR   Proteomes; UP000015042; 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   NCBIfam; NF040477; chlor_oxi_RclA; 1.
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.
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}.
FT   DOMAIN          5..301
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          328..435
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        426
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         165..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         292
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   441 AA;  47540 MW;  8A9F7D77BCCB5577 CRC64;
     MTQYQALIIG FGKAGKTLAA TLAKTGWRVA IIEQSPSMFG GTCINIGCIP TKTLVHDAER
     EADFSAAMQR KAAVVNFLRD KNFHNLADLH NVDVIEGRAE FIDNQTVRVV QAKGEQVLRG
     EKIFINTGAE SVIPAITGLT TTEGVFDSTG LLSLSERPAR LGILGGGYIG LEFASMFANF
     GTKVTIFEAA PQFLPREDRD IAQAIAHILQ EKGVELILNA KVQAVSSQAG AVQVELPEGA
     HLVDALLVAS GRKPATAGLQ LHNAGVAVNE RGGIIVDDYL RTTAENIWAM GDVTGGLQFT
     YISLDDFRIV RDGLLGEGKR STRDRQNVPY SVFMTPPLSR IGMTEEQARA SGATVQVVTL
     PVAAIPRARV IDDTRGVLKA VVDVNTQRIV GASLLCADSH EMINIVKTVM DADLPYTVLR
     DQIFTHPTMS ESLNDLFSLI K
//
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