ID A0A1W2TFT5_ROSNE Unreviewed; 458 AA.
AC A0A1W2TFT5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN ORFNames=SAMD00023353_2400840 {ECO:0000313|EMBL:GAP86934.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP86934.1};
RN [1] {ECO:0000313|EMBL:GAP86934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP86934.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU361137}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR EMBL; DF977469; GAP86934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TFT5; -.
DR STRING; 77044.A0A1W2TFT5; -.
DR OMA; TMEFESF; -.
DR OrthoDB; 5483022at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
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; 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; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE 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:RU361137,
KW ECO:0000313|EMBL:GAP86934.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:GAP86934.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:GAP86934.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 34..110
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 177..214
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 133..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 48237 MW; D3AFE3445BDCE226 CRC64;
MYGAVLRRQG LLRASALRSG LSPLARYYAS FPPHTIIKMP ALSPTMTAGN IGAWQKKAGD
TIAPGDVLVE IETDKAQMDF EFQEEGIIAK VLKDAGEKDV TVGNPIAVLV EEGTDISAFE
SFTLADAGGD AAAPAASKET KSDNSAASSA PAPTSAPEPT EYASEGRIQT ALDREPNISA
AAKRLARENG VSVGSLKGTG PGGRITEEDV KKASSGASGA VSAAASYVDT PLTNMRKTIA
KRLQESSQNN PHFFVTSKVS ASKLLKLRQA LNSSAEGKYK LSVNDFIIKA MAVASKKVPA
VNSSWQGDSI RQYNNVDISV AVATPTGLIT PIVTNVEGRG LESISSTVKE LAKKARDNKL
KPHEYQGGTI SLSNMGMNSA VDHFTAIINP PQAAILAVGT TKKVPIAVEG EDGSSSIEWD
DQITVTASFD HRVVDGAVGG EWIKEFKKVV ENPLELLL
//
