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Database: UniProt
Entry: Q0CIX3_ASPTN
LinkDB: Q0CIX3_ASPTN
Original site: Q0CIX3_ASPTN 
ID   Q0CIX3_ASPTN            Unreviewed;       481 AA.
AC   Q0CIX3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 93.
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=ATEG_06361 {ECO:0000313|EMBL:EAU32905.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU32905.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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; CH476602; EAU32905.1; -; Genomic_DNA.
DR   RefSeq; XP_001215539.1; XM_001215539.1.
DR   AlphaFoldDB; Q0CIX3; -.
DR   STRING; 341663.Q0CIX3; -.
DR   EnsemblFungi; EAU32905; EAU32905; ATEG_06361.
DR   GeneID; 4321875; -.
DR   VEuPathDB; FungiDB:ATEG_06361; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; 5483022at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IEA:EnsemblFungi.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:EnsemblFungi.
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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:EAU32905.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          57..133
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          200..237
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          145..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  51540 MW;  B97D005AAF482EDF CRC64;
     MVASAVRMRA PSAMFLKGAS SLRRPQAVHR FKETIQPQLP AFSALSRFYA SKSFPPHTII
     SMPALSPTMS AGNIGAWQKK AGDTLAPGDV LVEIETDKAQ MDFEFQEEGV LAKVLKETGE
     KDVAVGSPIA VLVEEGTDVA PFESFSLEDA GGDKPAAAQE SKEEPKGEAA PAPTPAPEPA
     AEEPEYNGEK LQPSLDREPS ISPAAKALAL EKGVPIKALK GTGRGGQITK EDVEKYKPTA
     VAAEAPYEDI PLTSMRKTIA TRLQQSMREN PHYFVSTTLS VSKLLKLRQA LNASSNGQYK
     LSVNDFLVKA CAIALRKVPA VNSSWREENG QVVIRQHNTA DISVAVATPN GLITPVVKNV
     GGLGLSNISN QIKDLGKRAR DNKLKPEEYQ GGTFTISNMG MNAAVERFTA VINPPQAGIL
     AVGTTRKVAV PVETEEGTAV EWDDQIVVTG SFDHKVVDGA VGAEWIKELK KVVENPLEML
     L
//
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