ID U4KXM0_PYROM Unreviewed; 409 AA.
AC U4KXM0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Similar to Pyruvate dehydrogenase complex protein X component, mitochondrial acc. no. P16451 {ECO:0000313|EMBL:CCX06561.1};
GN ORFNames=PCON_06148 {ECO:0000313|EMBL:CCX06561.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX06561.1};
RN [1] {ECO:0000313|EMBL:CCX06561.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX06561.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX06561.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR EMBL; HF935296; CCX06561.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KXM0; -.
DR STRING; 1076935.U4KXM0; -.
DR eggNOG; KOG0557; Eukaryota.
DR OMA; DGIMMKI; -.
DR OrthoDB; 52212at2759; -.
DR Proteomes; UP000018144; 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:CCX06561.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 29..105
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 165..202
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 142..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 43365 MW; 59E31D4740CEF656 CRC64;
MASLHRLTAP LRRQVLTRGF RTATPHNAAQ PMMMPAMSPT MTEGAISSWK VKEGEAFAAG
DVLLEIETDK AQMDVEAQDD GVMAKIIIPG GTKNIAVGTR IAVLAEEGDD LATLEIPADK
NTEKAKESIT PQAAKIVRVA NETPKTTEAS AESTPETSHT KVPTHPSPSV LSLLKSNNLD
AALIKGSGPK GRLLKGDVLA HLGRISKSAP TDLSNRIKTL SKLDLSNIKV AAPKPAPAPA
KKPEPKKAAP PPAPKLAELS LPVSFANILA ASQRRNIPLS QTINAAITHA NASLPAQKTA
PTQDELFNDL LGLPNKPRRA TVGSYAPTIT PLPRPGAAIS VQPRSVDIFD ELLGVSADII
NKRTQPRDGI IAGGENLVAL KVQECERERA RVFLDRFKAA VERGAEALV
//
