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Database: UniProt
Entry: A0A2C5YYK5_9HYPO
LinkDB: A0A2C5YYK5_9HYPO
Original site: A0A2C5YYK5_9HYPO 
ID   A0A2C5YYK5_9HYPO        Unreviewed;       459 AA.
AC   A0A2C5YYK5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-JUN-2019, entry version 8.
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=CDD83_7590 {ECO:0000313|EMBL:PHH92409.1};
OS   Cordyceps sp. RAO-2017.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH92409.1, ECO:0000313|Proteomes:UP000221130};
RN   [1] {ECO:0000313|Proteomes:UP000221130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA   de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHH92409.1, ECO:0000313|Proteomes:UP000221130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1346 {ECO:0000313|EMBL:PHH92409.1,
RC   ECO:0000313|Proteomes:UP000221130};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of
RT   potential behavioral manipulation genes and a possible major role for
RT   enterotoxins.";
RL   Submitted (OCT-2017) 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=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, 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 matrix
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PHH92409.1}.
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DR   EMBL; NJEV01000045; PHH92409.1; -; Genomic_DNA.
DR   OrthoDB; 747232at2759; -.
DR   Proteomes; UP000221130; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; 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:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 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   Complete proteome {ECO:0000313|Proteomes:UP000221130};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN       36    112       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      179    216       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      128    167       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2C5YYK5}.
SQ   SEQUENCE   459 AA;  48955 MW;  691787CC82BA2376 CRC64;
     MLSAALRRRA LAPTRSALRT GFTAHVVRRY ASFPDHQVVK MPALSPTMQA GNIGAWQKKP
     GDSIAPGDVL VEIETDKAQM DFEFQEEGVI AKILKDSGDK DVPVGSPIAV LVEEGTDIAA
     FESFTLKDAG GDAQPAQPKK EDKTESQPQQ SSAPEPSPEP EQYAPSAGKL QTALEREPNI
     GPAAKRLARE KGISLDGLKG TGKGGKITEE DVKKAVGSPA AASPGATFED VPVSGMRKTI
     AGRLQESVQK NPHFFVTSSV SVSKLLKLRQ ALNSSAEGKY KLSVNDFLIK AMAAACKKVP
     TVNSSWREDS IRQFNTVDVS VAVSTPSGLI TPIVTGVDAR GLESISARVK ELAKKARDNK
     LKPEEYQGGT ISISNMGMND AIDHFTAVIN PPQAAILAVG TTKKVAIPVE NEDGTTGVEW
     DDQITVTGSF DHKVVDGAVG AEWMRELKKI IENPLNLVL
//
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