ID A0A420Y1P7_9PEZI Unreviewed; 339 AA.
AC A0A420Y1P7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=KGD2 {ECO:0000313|EMBL:RKU41709.1};
GN ORFNames=DL546_003065 {ECO:0000313|EMBL:RKU41709.1};
OS Coniochaeta pulveracea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU41709.1, ECO:0000313|Proteomes:UP000275385};
RN [1] {ECO:0000313|EMBL:RKU41709.1, ECO:0000313|Proteomes:UP000275385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAB683 {ECO:0000313|EMBL:RKU41709.1,
RC ECO:0000313|Proteomes:UP000275385};
RA Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL Submitted (AUG-2018) 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 -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145}.
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:RKU41709.1}.
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DR EMBL; QVQW01000069; RKU41709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420Y1P7; -.
DR STRING; 177199.A0A420Y1P7; -.
DR Proteomes; UP000275385; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; 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 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; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 40..115
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 111..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 37200 MW; E17EE21AB8216FE6 CRC64;
MVYRGLRIAA RAASRISLTQ PQTSLYRLPT QFHQVRTYAD TIIKVPQMAE SISEGTLKQF
NKQIGDYVEQ DEEIATIETD KIDVAVNAPE AGTIKEFLAN EEDTVTVGQD LVRLESGGAP
KKTEAKESPK EEKKETPAPE KKSEPESKPE PKQESKPAPP QPKQESKPAK PEPKQSEKSS
QPQKDVSTLG SREERRVKMN RMRLRIAERL KQSQNTAASL TTFNEVDMSA LMAFRSKYKE
EVLKKTGVKL GFMSAFSRAA VLAMRDIPAV NASIEGPNGG DTIVYRDYVD ISVAVATEKG
LVTPVVRNVE AMDLVGIESS IAELGKKVRA SANAASPLG
//
