ID A0A0B1P859_UNCNE Unreviewed; 428 AA.
AC A0A0B1P859;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 03-MAY-2023, entry version 29.
DE SubName: Full=Putative pyruvate dehydrogenase protein x component {ECO:0000313|EMBL:KHJ32809.1};
GN ORFNames=EV44_g2964 {ECO:0000313|EMBL:KHJ32809.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ32809.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ32809.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHJ32809.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNVN01001804; KHJ32809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1P859; -.
DR STRING; 52586.A0A0B1P859; -.
DR HOGENOM; CLU_035825_2_0_1; -.
DR OMA; DGIMMKI; -.
DR OrthoDB; 52212at2759; -.
DR Proteomes; UP000030854; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF82; PYRUVATE DEHYDROGENASE COMPLEX PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Pyruvate {ECO:0000313|EMBL:KHJ32809.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030854};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 37..116
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 176..216
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 132..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 46551 MW; 33DE3F960A386BD7 CRC64;
MASLSSVCRL NVRLMARKLP QKKIFRGLRT STTSHVAQNL TMPALSPTMT EGNIAKWNVK
EGDSFTAGDV LLQIETDKAS MDVEAQDDGV MAKIILGDDS KGIKVGTRIG VLADVGDDLS
KLEISIEDST SAIAPKEQSG PKIEDTNHAK SSATSESKLG SKPNSALNLG KKQAYPLLPS
VQHLIRLHNI DQSSIDKITP SGPNNRLLKG DVLAFLGQVS KSYPAQLSGK ISNLSHLDLS
NIRIKTPIIA TPKTAKTTET ISPTPEAMVI LEQPISFENI YEIQKKMKSI LGASLSEEKL
ISRATYLANK SVPRPKSYKT TKNELFEAVL GIDKKSTPKI QLFSPTIIPP SLSSACISKQ
NPAKKIDIID ILSGKKRPSS KLQINEIKSD SIHKIFKLEV AKSDEEKARI FLGTMKTTLE
SQPGNLIY
//
