ID A0A0P0UPU6_9GAMM Unreviewed; 467 AA.
AC A0A0P0UPU6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 Name=pdhD {ECO:0000313|EMBL:BAS67192.1};
GN ORFNames=BSEPE_0168 {ECO:0000313|EMBL:BAS67192.1};
OS endosymbiont of Bathymodiolus septemdierum str. Myojin knoll.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS67192.1, ECO:0000313|Proteomes:UP000067399};
RN [1] {ECO:0000313|EMBL:BAS67192.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67192.1,
RC ECO:0000313|Proteomes:UP000067399};
RA Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., Hashimoto J.;
RT "Phylogenetic characterization of endosymbionts in three hydrothermal vent
RT mussels: influence on host distributions.";
RL Mar. Ecol. Prog. Ser. 208:147-155(2000).
RN [2] {ECO:0000313|EMBL:BAS67192.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67192.1,
RC ECO:0000313|Proteomes:UP000067399};
RX PubMed=26418631; DOI=10.1038/ismej.2015.176;
RA Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S.,
RA Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., Tamotsu H.,
RA Hirano T., Maruyama T., Yoshida T.;
RT "Heterogeneous composition of key metabolic gene clusters in a vent mussel
RT symbiont population.";
RL ISME J. 10:990-1001(2016).
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; AP013042; BAS67192.1; -; Genomic_DNA.
DR RefSeq; WP_066042678.1; NZ_AP013042.1.
DR AlphaFoldDB; A0A0P0UPU6; -.
DR STRING; 1303921.BSEPE_0168; -.
DR KEGG; ebh:BSEPE_0168; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000067399; 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:UP000067399}.
FT DOMAIN 5..323
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 342..447
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 177..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 314..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 467 AA; 49706 MW; DA2D21F59EE597C6 CRC64;
MIKTQVVVIG SGPGGYTAAF RAADLGKQVV LIERYESLGG VCLNVGCIPS KALLHTAEII
NEAAEAKHLG VTFGSPEISI DGVRKNKDAV VAKLTDGIKA LANARKVKVV KGYGKFISNT
QIAIEGSDEI VEFEQCIIAA GSRVSKIPAF PFDDPRVMDS TDALELDSVP KRLLVVGGGI
IGLEMATVYA ALGSEITVVE LSDQLIAAAD KDIVAPLFKR IKKQYENIFL NTKVTSMDAQ
NDGIKVGFEG KNAPETDTFD KVLVSIGRSA NGKLIDANKA GVNVDDWGFI KVDKQMKTNV
ENIYAIGDIV GQPMLAHKAV HEAKVAAEVI CGHKSGFDAL TIPSVAYTDP EVAWTGKTEK
ELKAEGIDYE VGKFPWAASG RSLSIGRSEG ISKALFDKHT HRILGMGICG TNAGELIAEP
TLAIEMGCDM SDIALTIHAH PTLSETTAFA VEMAEGTITD LLPPKKR
//
