ID G5QW74_SALSE Unreviewed; 365 AA.
AC G5QW74;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:EHC93133.1};
DE Flags: Fragment;
GN ORFNames=LTSESEN_0933 {ECO:0000313|EMBL:EHC93133.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC93133.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC93133.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC93133.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EHC93133.1}.
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DR EMBL; AFCU01000301; EHC93133.1; -; Genomic_DNA.
DR AlphaFoldDB; G5QW74; -.
DR PATRIC; fig|913082.3.peg.734; -.
DR Proteomes; UP000005065; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; 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 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 4: Predicted;
FT DOMAIN 7..227
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 252..359
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHC93133.1"
SQ SEQUENCE 365 AA; 39577 MW; 29665FB64046D363 CRC64;
FLRDKNFHNL ADLDNVDVIE GRAEFIDNHT LRVFQADGER VLRGEKIFIN TGAESVIPAI
TGLTTTAGVF DSTGLLSLSQ RPARLGILGG GYIGLEFASM FANFGTKVTI FEAAPQFLPR
EDRDIAQAIT RILQEKGVEL ILNANVQAVS SREGAVQVET PEGAHLVDAL LVASGRKPAT
AGLQLQNAGV AVNERGGIIV DDYLRTSADN IWAMGDVTGG LQFTYVSLDD FRIVRDGLLG
DGKRSTRDRQ NVPYSVFMTP PLSRVGLTEE QARASGATVQ VVTLPVAAIP RARVMNDTRG
VLKAVVDVNT QRIVGVSLLC VDSHEMINIV KTVMDADLPY TVLRDQIFTH PTMSESLNDL
FSLIK
//
