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Database: UniProt
Entry: H0ETR5_GLAL7
LinkDB: H0ETR5_GLAL7
Original site: H0ETR5_GLAL7 
ID   H0ETR5_GLAL7            Unreviewed;       390 AA.
AC   H0ETR5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   SubName: Full=Putative Pyruvate dehydrogenase complex protein X component, mitochondrial {ECO:0000313|EMBL:EHK98084.1};
GN   ORFNames=M7I_6133 {ECO:0000313|EMBL:EHK98084.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK98084.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK98084.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
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:EHK98084.1}.
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DR   EMBL; AGUE01000165; EHK98084.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0ETR5; -.
DR   HOGENOM; CLU_035825_2_0_1; -.
DR   InParanoid; H0ETR5; -.
DR   Proteomes; UP000005446; 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   Pyruvate {ECO:0000313|EMBL:EHK98084.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..65
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          135..175
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          66..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  41232 MW;  87BE40CECF25FE28 CRC64;
     MTEGNIASWK VKEGDSFSAG DVLLEIETDK ASMDVEAQDD GIMAKITQGD GTKGIKVGSR
     IGVIAESGDD ISSLEIPAEE KPEAPSPKEE SAKPNKETTS ESQAEAPPTS KPSSSAGESK
     PQKKSSGPAK KQTKPLLPSV QALIHEKGLE QADVDKMTPS GPNNRLLKGD VLAYLGTVSE
     SYPTELAGKI EKLMHLDLSN IKLAAPAPKP QKEVKQAEKP VAEVPSRVAV SISMASVIEV
     QSRVQKTLGV FMPLSTFISR ATDIANDNLP KSKTYQPSAD ELFNDILGIN KVTTSSGVRG
     SFLPQITALP TSAPLAPVKS LPARSSDIID ILSGTTKRKS PALAARPVPG LSNAVNVFSV
     SVPKGDEKRA RIFLGRVKSV LETEPGRLVL
//
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