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Database: UniProt
Entry: A0A0D2APS4_9PEZI
LinkDB: A0A0D2APS4_9PEZI
Original site: A0A0D2APS4_9PEZI 
ID   A0A0D2APS4_9PEZI        Unreviewed;       455 AA.
AC   A0A0D2APS4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=PV09_00645 {ECO:0000313|EMBL:KIW08698.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08698.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW08698.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08698.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; KN847530; KIW08698.1; -; Genomic_DNA.
DR   RefSeq; XP_016218567.1; XM_016353414.1.
DR   AlphaFoldDB; A0A0D2APS4; -.
DR   STRING; 253628.A0A0D2APS4; -.
DR   GeneID; 27308618; -.
DR   VEuPathDB; FungiDB:PV09_00645; -.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   InParanoid; A0A0D2APS4; -.
DR   OrthoDB; 5483022at2759; -.
DR   Proteomes; UP000053259; 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: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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:KIW08698.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KIW08698.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          51..127
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          141..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  47904 MW;  86A990C0F0012E0F CRC64;
     MATLSRASSR IPLWSASRSV ARTVITNNAI ARTPALAALA RYYASKSYPP HTIISMPALS
     PTMTSGNIGA WQKKAGDSLS PGDVLVEIET DKAQMDFEFQ EEGVLAKILK ESGEKDVAVG
     SPIAVMVEEG EDISAFESFT VEDAGGDKAP PKEKPSAEAT ESSDPPKSTP KKSESAPAAA
     ESESTGGRLE TALSRFRKQP KEAAKSGAAP AATSAAPAAA TYVDEEPSSM RKTIAKRLQQ
     SMNENPHYFV TSAVSVTKLL KLRAALNASA NGAYKLSVND FLIKACAVAL AKVPAVNSAW
     IEQGGKAVIR RYTVADISVA VATPSGLMTP IIKNVGGIGL ASISAQVKDL GKRARDGKLK
     PDEYQGGTFT ISNMGMNDAV DRFTAVINPP QAAILAVGTT KKVAIPAEGE EGGVEWDDQI
     VLQCSFDHKV IDGAVGAEFM KELKKVVENP LELLL
//
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