ID I6S3W1_ENTHA Unreviewed; 468 AA.
AC I6S3W1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00016961, ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN OrderedLocusNames=EHR_12850 {ECO:0000313|EMBL:AFM71435.1};
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM71435.1, ECO:0000313|Proteomes:UP000002895};
RN [1] {ECO:0000313|EMBL:AFM71435.1, ECO:0000313|Proteomes:UP000002895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC {ECO:0000313|Proteomes:UP000002895};
RX PubMed=22933757; DOI=10.1128/JB.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00043836,
CC ECO:0000256|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC ECO:0000256|RuleBase:RU003692};
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000256|RuleBase:RU003692}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003692}.
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DR EMBL; CP003504; AFM71435.1; -; Genomic_DNA.
DR RefSeq; WP_010719369.1; NZ_KB946231.1.
DR AlphaFoldDB; I6S3W1; -.
DR GeneID; 56787734; -.
DR KEGG; ehr:EHR_12850; -.
DR PATRIC; fig|768486.10.peg.1127; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_1_9; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000002895; 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; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003692}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003692};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000002895}.
FT DOMAIN 11..330
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 349..457
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 447
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 148..150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 184..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 47..52
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 468 AA; 49202 MW; 46C2141944583B25 CRC64;
MVVGDFAVEL DTVVIGAGPG GYVAAIRAAE MGQKVAIIER EYIGGVCLNV GCIPSKALIA
AGHHYQESLD STLFGVTSEN VTLDFAKTQD WKENKVVKTL TSGVGFLLKK HKVETIEGEA
FFVDDHTLRV IHPDSAQTYS FNNAIIATGS RPIEIPGFKF GGRVLDSTGG LALKEVPKKF
VIIGGGVIGA ELGGAYANLG AEVTILEGSP QILPTYEKDM VKLVEDDFKK KGVTIVTNAM
AKEAVDNGDS VTVKYTVDGK EETVTADYVM VTVGRRPNTD DMGLEQAGVE VGERGLIPVD
QQGRTNVPNI FAIGDIVPGA ALAHKASYEA KIAAEAISGK KVAVDYKAMP AVAFTDPELA
SVGMTIKEAK EAGIEATAYK FPFSGNGRAL SLAKTEGFIR LVTTNEDNVI IGAQIGGVGA
SDMVSELALA IESGMNAEDI ALTIHPHPSL GEITMDAAEL ALGLPIHI
//
