ID W7HVV5_9PEZI Unreviewed; 483 AA.
AC W7HVV5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, 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=DRE_01360 {ECO:0000313|EMBL:EWC44008.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC44008.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC44008.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC44008.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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; KI966448; EWC44008.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HVV5; -.
DR HOGENOM; CLU_016733_10_0_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
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; 4.10.320.10; E3-binding 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; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 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 Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 46..121
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 182..219
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 125..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 51883 MW; 36B535D43D7785FE CRC64;
MWRRSLINRV RSSSSSSQAG YRSAWRLQLR AQQQLQLHTS RPVFEVKPFL LADIGEGIRE
CEIIQWFVQP GAKVQQFDNI CEVQSDKASV EISSRYDGVI KKLYYEAGDM ATVGKPLVDI
DMSESLDDDA PRTADAPVQP ASDSARAPLE SPAVVHTSTA TQTGVGAGGE EDGSRSERHR
SLATPAVRRL VKEQGLDITA ITGTGKDGRV LKEDVVRYVE TGASSAASGS ATYAGSAPVM
ASAQESVVPL TPVQSQMFKM MTKSLTIPHF LYADEATIDR LVALRASINR SLALTGNDRV
KKISYMPFFI KAVSAALLDF PVINSRVDLS DEAKPKLVMR PQHNVGVAMD TPTGLLVPNI
KNVQDLSILD IAAELGRLQA AGSAGKLGAA DLKGGTITVS NIGNVGGTYV APVIVTSEVA
IMGVGRTKVV PAFDEDGAVV PKTVVNFSWS ADHRVVDGST MARMASLVKR YCEEPELLIS
RLR
//
