ID R8ALY5_PLESH Unreviewed; 482 AA.
AC R8ALY5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:EON87322.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:EON87322.1};
GN ORFNames=PLESHI_16302 {ECO:0000313|EMBL:EON87322.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON87322.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON87322.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON87322.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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 -!- 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:EON87322.1}.
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DR EMBL; AQQO01000366; EON87322.1; -; Genomic_DNA.
DR RefSeq; WP_010864847.1; NZ_KB944511.1.
DR AlphaFoldDB; R8ALY5; -.
DR STRING; 703.SAMEA2665130_02833; -.
DR GeneID; 69704595; -.
DR PATRIC; fig|1315976.3.peg.3116; -.
DR HOGENOM; CLU_016755_0_3_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000014012; Unassembled WGS sequence.
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:EON87322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014012}.
FT DOMAIN 7..326
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 349..458
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 448
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 142..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 179..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 269
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 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 482 AA; 52508 MW; C6ABFC9F5A8F8FA1 CRC64;
MKQLQVDVAV IGGGTAGLGA YRAAKAHTAS VVMIEGGPYG TTCARVGCMP SKLLIAAAEA
VHQIEKAPGF GIHPNGKPQI NGVEVMDRVK RERDRFVGFV LEGVDSIPAE DKIAGYARFI
DAHTLQVDDH TQIQAKRIVI ATGSRPSWPA AWNSLGDRLI INDDVFNWDT LPRSVAVFGP
GVIGLELGQA LHRLGVNVVM FGMGGLVGPL TDSAIRDYAE RALNQEFYLD ADAKVERMER
EGEQVFIRYQ DKQGQMQEIL VDYVLAATGR RPNVDNLGLE NTALELDSRG VPQADRYTMQ
TSVPHIFIAG DASNQLPLLH EASDQAKIAG DNAGRFPDLR AGLRRSAISV VFSDPQIAMV
GSTHRELTAR YGSCGCFATG EVSFENQGRS RVMLRNKGML HVYGEQGTGR FLGAEMMGPD
AEHIAHLLAW AHQQQMTVSQ MLDMPFYHPV IEEGLRTALR DLQAKLKLGP EMVAHCQTCP
GE
//
