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Database: UniProt
Entry: E6ZL03_SPORE
LinkDB: E6ZL03_SPORE
Original site: E6ZL03_SPORE 
ID   E6ZL03_SPORE            Unreviewed;       490 AA.
AC   E6ZL03;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=sr11872 {ECO:0000313|EMBL:CBQ68006.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ68006.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ68006.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
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; FQ311430; CBQ68006.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZL03; -.
DR   EnsemblFungi; CBQ68006; CBQ68006; sr11872.
DR   VEuPathDB; FungiDB:sr11872; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   OrthoDB; 5483022at2759; -.
DR   Proteomes; UP000008867; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006412; P:translation; 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; IPR001859; Ribosomal_P1/P2_euk.
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   PRINTS; PR00456; RIBOSOMALP2.
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:CBQ68006.1};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          41..117
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          179..216
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          132..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  50952 MW;  6D20D304C925C0D4 CRC64;
     MQALRALQRS GLQKAVSAAS SSSSSTLSQR SFHSSRRALE FSKFNMPAMS PTMTEGGIAA
     WKKKPGEAFS AGDVLLEIET DKATMDVEAQ DDGVLAKILV GDGSKAVQVN SLIAIMAEEG
     DDLSGADAFA DKAASEAGDA KPAEQPKKEE SAPAESSSSS SSSSSGSSFG SQSSGDRIFA
     TPVARRLAQD KGIALNKIKG TGPDGRIIKA DVENYKPEAA AAAAPAASKS ASSAAAAPAK
     SAPAPASSEG DYTDIPVSNM RRTIAARLTE SKSTVPHYYV SIDVEMDKVL KLREVFNKAA
     AEKAGKDVEK AKAAKLSVGD FITKAAGVAL KEVPEVNSAW YGDFIRQHNK ADISIAVSTP
     TGLITPIVKD VGGSGLATIS AATKQLAAKA RAGKLAPHEY QGGSFTISNM GMFGITHFTA
     IINPPQSCIL AIGGTEARLI PDAESEQGFR KSMVMQATIS ADHRTVDGAT AAKWMKAFKD
     ALENPLSFML
//
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