ID F0JBA9_NEOCL Unreviewed; 648 AA.
AC F0JBA9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Dihydrolipoyl dehydrogenase, related {ECO:0000313|EMBL:CCA30138.1, ECO:0000313|EMBL:CEL71376.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:CEL71376.1};
GN ORFNames=BN1204_070190 {ECO:0000313|EMBL:CEL71376.1}, NCLIV_070190
GN {ECO:0000313|EMBL:CCA30138.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307;
RN [1] {ECO:0000313|EMBL:CCA30138.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CCA30138.1};
RA Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA Wastling J.M., Pain A.;
RT "Comparative genomics and transcriptomics of Neospora caninum and
RT Toxoplasma gondii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCA30138.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CCA30138.1};
RA Aslett M.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CEL71376.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CEL71376.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CADU01000338; CCA30138.1; -; Genomic_DNA.
DR EMBL; LN714488; CEL71376.1; -; Genomic_DNA.
DR AlphaFoldDB; F0JBA9; -.
DR VEuPathDB; ToxoDB:NCLIV_070190; -.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 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.
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|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 151..507
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 526..637
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 98..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 67781 MW; F91AE97EB969897C CRC64;
MSFGFCLRRC GVGRTLLGVS PFPCRGFLER KARDTRLFLT ALLFTVSTVA TFSACLATQR
SAVLSQVYPV RLSIPPGSGQ RSASFVPSPT PPFFLRASLQ DSPGVRTPQP HNTVHSRRLQ
SLASDTAPHL AGGGVSPLSA TAGPSGSNEP FDVTIIGLGV GGHAAALHAA ALGLKTAVVS
GGDPGGTCVN RGCVPSKALL AAARRVKMLR NKHHLAAMGL EIEGGRVTVD PVGVGSHAKG
VVDKVRSGLI GSLASHGIAL FDARGVLNGE PGRVVLERTA GSPASLPSSI LTKNIILAPG
SLPFVPPGVT FDEAQHQVMT SDTCVTLPWL PSEVCIVGSG YIGLEFMDVF TSLGSEVVMV
EAGPRLLPGV DKEIAKLAER LLLQQFKERP VKLYTNTLAS QVRPLGPKGE APVEVELTDA
KTKERKGKIY PDACLIATGR KPNTQGLGLD SLGVTLKRGG FIPVDACMRV LKHAPEGDEK
PEVIQGVYCV GDANGQMMLA HAASAQAIAA VETIAGRPRT VNVKHIPAAC FTSPEIAFIG
DTEEAAVELG AREGFEVGKS VSHFRANTKA IAEGEGDGIL KVLYRKDTGK ILGCHMIGIH
ASDLIQECAT AITNGISVKD LAFTVHTHPT LSEVVDAAWK KAAGMNAH
//
