ID A0A0G4G533_VITBC Unreviewed; 500 AA.
AC A0A0G4G533;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN ORFNames=Vbra_17014 {ECO:0000313|EMBL:CEM23213.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM23213.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM23213.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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|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; CDMY01000562; CEM23213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4G533; -.
DR STRING; 1169540.A0A0G4G533; -.
DR VEuPathDB; CryptoDB:Vbra_17014; -.
DR InParanoid; A0A0G4G533; -.
DR OMA; CAQLGMK; -.
DR OrthoDB; 5473641at2759; -.
DR PhylomeDB; A0A0G4G533; -.
DR Proteomes; UP000041254; 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:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 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:UP000041254}.
FT DOMAIN 31..360
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 78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 171..173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 210..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 351..354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 69..74
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 500 AA; 52511 MW; E03832EBB6737444 CRC64;
MMLRSGRSGL QSPPFHRAFQ NASRGFASEA YDVAVIGGGP GGYVAAIKSA QLGLKTVCVE
KRGALGGTCL NVGCIPSKAL LNISHKYHEM LHDYAKMGIS FDNPAFDVAK MMAQKEKSVK
GLTGGIEFLF KRNKVDYIKG WGKLTGPTEV SVDLNEGGSK QLSAKNIIIA TGSDPAPMPG
GSLVADEKTI LTSTGAIALE DVPKKMVVVG GGYIGLELGS VWGRLGAEIE VVEFTDKIAG
TLDGEVGKAF QKTLEKQGMK FHLGTKVVGA EVHANGATVI TEPAKGGAQS KIECDKILLS
VGRVPFTEGL GLEQLGVTKD KMGRVDVDPH TFQVPNFPSL RAIGDVIVGP MLAHKAEEEG
IAAVELIAGQ GAGHVNYNAI PGVVYTHPEV AGVGLTEEQC KEQKIAYKKG SFPFAANSRA
RTNDDSEGLV KVITEAESDK VIGAHMIGPN AGELIAEMVL AIEYGAASED VARTCHAHPT
LSEAVKEACM AAHGKPIHFG
//
