ID A0A0R3PIK1_ANGCS Unreviewed; 248 AA.
AC A0A0R3PIK1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608};
DE EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608};
GN ORFNames=ACOC_LOCUS4179 {ECO:0000313|EMBL:VDM55764.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000417801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000417801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM55764.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM55764.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|ARBA:ARBA00043836};
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DR EMBL; UYYA01002355; VDM55764.1; -; Genomic_DNA.
DR STRING; 334426.A0A0R3PIK1; -.
DR WBParaSite; ACOC_0000417801-mRNA-1; ACOC_0000417801-mRNA-1; ACOC_0000417801.
DR OMA; ICERAGH; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
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 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 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027}.
FT DOMAIN 43..115
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 134..235
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 248 AA; 27568 MW; DC6C668EE8DA3C75 CRC64;
MSPLCYIMLL KQGGGLDLEW YRELPAMEST SSLKWKVQKM GRNRKDLQLE CDTLLVSIGR
RPYTKDLGLE SVSINLDERG RVPVNERFQT KVPSIYAIGD CIAGPMLAHK AEDEGILCVE
GICGGPVHID YNCIPSVIYT HPEVAWVGKP EEQLKQEGVE YKVGKFPFVA NSRAKTNFDT
EGFVKVLADK QTDRMLGVHI IGPNAGEMIA EGTLALEYGA SAEDVARVCH PHPVSTFWPA
ERFLVFNV
//
