ID A0A0W8DNM9_PHYNI Unreviewed; 942 AA.
AC A0A0W8DNM9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=AM587_10009538 {ECO:0000313|EMBL:KUF97714.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF97714.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF97714.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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:KUF97714.1}.
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DR EMBL; LNFO01000919; KUF97714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8DNM9; -.
DR STRING; 4790.A0A0W8DNM9; -.
DR EnsemblProtists; KUF97714; KUF97714; AM587_10009538.
DR OMA; ANCFFDI; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:KUF97714.1};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..65
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 410..666
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 86..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 892..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 842..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 942 AA; 101946 MW; 79E600457D33EC3A CRC64;
METGSLSSWL KKEGEEVSAG EVLCQVETDK AVVDYEMQDD AVVAKIICPE GSADLPIGAL
LAYTVEDMDT YKQLLDSGAL ANLSAEAPSA SEPVAESKPE PTPASTPAAE SNHSGRVPLI
KFLGKRSLLP EFNHSPLEEP AKPASAAPAA QPVATSTVAA DAEYEDLPLS NMRKIIAKRL
AASKQEVPHS YTSIDCEIDS ILKFRKQLKT KHDVKVGMND FILKAVALAL RDVPEANCFF
DVKTQRVQPN ASVDVSVAVA TATGLITPIV PKVDTLGLSG VNSIFMELVT RARQNKLKPE
EFQGGSFTVS NLGSFGIDQF RAVINPPQAC ILAVGGGRKE VLPPLEIVEG VNPEPRIATL
MNVTLSSDRR VVDGVIAGQF LQAFKAYMEN PELMVLMASI QRNENPEGVY EVLERIGEGS
YGKVYKAVNK SNAEVVALKV VPVESEDRAA FDELTREIRI LERCESPFVV HYRGSFSYES
QLWIAMEFCA AGSLADLHVL RGRRVLSEPE IAAVCANVAL GLAHLHSQGL IHRDIKAGNL
LLNGDGVAKL ADFGVSAQLT ATVGKRRTVI GTPFWMAPEV IQEAHYDCKA DLWSLGITAL
ELAEGEPPLA HMHPMRAIFL IPNRAPPELR EPNKYSTEFR DFIAVCLKKD PQERASADEL
LRHPFIARSV ERLRANSGRA GNGGRMAGLP VLQELVEQSL ELVHEARLRG AEDEAEFRDA
ATGRPDGSLS VADLSTMLRN GSLLNGTGGF GGFGGSDTAV GFSSMRLNGF GGTTVFSNAG
GEDGCGTMVY RGDDNKSTNS TMESTSSETR EREITSSDLY GTMIPISASG TVRPPPAPVA
PVSNSRTSSR SSRESSQGET TKPEAESNEP SFMKYFRRIT SSSSKSGTIR AAGATEASLR
TVQQKLRQLE EDYERDREEL ARRFEKQKAE LERELESLGF TS
//
