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Database: UniProt
Entry: G2H0J5_9ENTR
LinkDB: G2H0J5_9ENTR
Original site: G2H0J5_9ENTR 
ID   G2H0J5_9ENTR            Unreviewed;       507 AA.
AC   G2H0J5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   ORFNames=Rin_00015740 {ECO:0000313|EMBL:EGY28486.1};
OS   Candidatus Regiella insecticola 5.15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Regiella.
OX   NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY28486.1, ECO:0000313|Proteomes:UP000004116};
RN   [1] {ECO:0000313|EMBL:EGY28486.1, ECO:0000313|Proteomes:UP000004116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116};
RX   PubMed=21948522; DOI=10.1101/gr.125351.111;
RA   Hansen A.K., Vorburger C., Moran N.A.;
RT   "Genomic basis of endosymbiont-conferred protection against an insect
RT   parasitoid.";
RL   Genome Res. 22:106-114(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:ARBA00001492,
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}.
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:EGY28486.1}.
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DR   EMBL; AGCA01000371; EGY28486.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2H0J5; -.
DR   PATRIC; fig|1005043.3.peg.1448; -.
DR   Proteomes; UP000004116; 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; 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};
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:UP000004116}.
FT   DOMAIN          41..361
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          380..488
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        478
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         150
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         216..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         305
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         346
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         352..355
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        78..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   507 AA;  53938 MW;  053D995FF7839222 CRC64;
     MSVDILGYSV IRANPRGSFK GEGYTRQKMQ EGMMSTKIET QVVVIGAGPA GYSAAFRCAD
     LGLKTVLVEY HPTLGGVCLN VGCIPSKALL HVAKVINEAK ALGNHGIAFG EPSIDLDKVR
     GWKEKVISQL TGGLAGMAKG RKVNVVNGKG KFTSANTLEV KNTAGAITTI TFDNAIIAAG
     SHPTALPFIP YEDPRIWDST DALKLKSVPK KLLIMGGGII GLEMATVYRA LGSEIDVVEM
     FDQVIPAADK DVIKVFTKKI SKQFNLMLET KVTKVEAKTD GVYVTMEGKK APKPQCYDAV
     LVAVGRVPNG KSLDAETAGV KVSEQGFINV DKQLRTNVPH IFAIGDIVGQ PMLAHKGVHE
     GHVAAEVIAG KKHYFDPKVI PSIAYTEPEV AWVGVTEKEA KEKGISFETA TFPWAASGRA
     IASDCAEGIT KLIFEKETRR IIGGAIVGSN GGELLGEIGL AIEMGCDAED LALTIHAHPT
     LHESVGLAAE IFEGSITDLP NPKAKKK
//
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