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Database: UniProt
Entry: A0A0F9X5G6_TRIHA
LinkDB: A0A0F9X5G6_TRIHA
Original site: A0A0F9X5G6_TRIHA 
ID   A0A0F9X5G6_TRIHA        Unreviewed;       411 AA.
AC   A0A0F9X5G6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   RecName: Full=Pyruvate dehydrogenase E2 component (Dihydrolipoamide acetyltransferase) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=THAR02_08042 {ECO:0000313|EMBL:KKO99849.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKO99849.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
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:KKO99849.1}.
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DR   EMBL; JOKZ01000294; KKO99849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9X5G6; -.
DR   OMA; DGIMMKI; -.
DR   OrthoDB; 52212at2759; -.
DR   Proteomes; UP000034112; 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   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          18..94
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          153..193
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          106..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  43551 MW;  A5272A256E4DA07A CRC64;
     MAWPFSTGFT TSSRCLAAQN FTMPALSPTM TEGNIASWKV KEGDSFSAGD VLLEIETDKA
     TMDVEAQDEG IMMKIISQDG SKSVQVGTRI AVLADAGDDI STLELPADEQ PQQSAQSTSQ
     PSAPAPREEP KSAAKPSAKP ESAASGTYEH NYPLLPSVSL LIHEHGISKE DLSKIKGTGP
     SGRLLKGDVL AFIGAINADR PAQVSSHFSK LAHLDLSNIK VAEKKAPAPK ASEAASKAPK
     AAPKEEKVLV QVPISLENVV QLQRRLQDSA DVSVSTATFI SKATAFANSR LPAVPHAPTA
     SELFDEVLGL GKAKATKFSQ GAYVPTIPDY SFTASRRASA PKSDIIDILT GPAKKSSSSS
     AQRASPRLDA RLAADGIHTF SLLVPKEEKA RAELFLERCK LALEEVPETL I
//
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