ID A0A1A8VTD6_PLAMA Unreviewed; 594 AA.
AC A0A1A8VTD6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Dihydrolipoyl dehydrogenase, apicoplast, putative (ALipDH) {ECO:0000313|EMBL:SBS82942.1};
GN ORFNames=PMALA_004980 {ECO:0000313|EMBL:SBS82942.1};
OS Plasmodium malariae.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5858 {ECO:0000313|EMBL:SBS82942.1, ECO:0000313|Proteomes:UP000078597};
RN [1] {ECO:0000313|Proteomes:UP000078597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; FLQW01000268; SBS82942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8VTD6; -.
DR VEuPathDB; PlasmoDB:PmUG01_05030800; -.
DR OMA; WASMLND; -.
DR Proteomes; UP000078597; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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 8..421
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 453..583
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 318..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 65703 MW; 1867FB5EF24E9A03 CRC64;
MAIDEKEYDI AILGCGVGGH AAAINAMERN FKVLIFVGEE NSIGGTCVNV GCIPSKSLLY
ATNKYRELKN MAKMYNYGIY SNLFLNEAHR KDGSDDNSSS SRSIRSSLSS LSSLSEHDKM
RSNQLVADSV EMDVEKLKEY TDSVISKLRG GITHGLQKSK FSKNSEHVQV IYEHGYIIDK
NTIKGKKSGN TYKVKNIILA TGSTPNIPEN VEVDEKSVFT SDQAVKLEGL RSYMSIIGMG
IIGLEFSDIY TALGSEITFF EYSPELLPMI DSDVANYFEK VFLQNKPVNY YLNSEIKYVK
ASKNNKPVIV GYVERGLTGG SSSSSSSSSS SSSSSDSSGT SIPSQIKELH VDSCLVATGR
KPNTQNLGLE NIETQINNRG YILVDDYLRV KKKNDEIYDN VFCIGDANGK QMLAHTASYQ
ALKVIDLIEM KEKNILKESA KNNINKPILY KNIPSVCYTN PELSFIGLNE KEANKMYADN
VGTAISYYKS NSKILCENNI TLHGQDKNNA YNKGQYNITD NTNGMVKIVY KKDTKEVLGM
FIVGNYASIL VHEAVLAINL GLTAHDLAYM VHSHPTVSEI LDTTFKAISK IRTH
//
