GenomeNet

Database: UniProt
Entry: A0A0D9N2I4_ASPFA
LinkDB: A0A0D9N2I4_ASPFA
Original site: A0A0D9N2I4_ASPFA 
ID   A0A0D9N2I4_ASPFA        Unreviewed;       571 AA.
AC   A0A0D9N2I4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=AFLA70_82g003350 {ECO:0000313|EMBL:KJJ34385.1};
OS   Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392242 {ECO:0000313|EMBL:KJJ34385.1, ECO:0000313|Proteomes:UP000032444};
RN   [1] {ECO:0000313|Proteomes:UP000032444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-384 / AF70 {ECO:0000313|Proteomes:UP000032444};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus flavus AF70.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC         Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001041};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJJ34385.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JZDT01000303; KJJ34385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9N2I4; -.
DR   OrthoDB; 1000728at2759; -.
DR   Proteomes; UP000032444; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF11; PYRUVATE DECARBOXYLASE; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:KJJ34385.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..110
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          207..317
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          407..483
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         476
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         478
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   571 AA;  62765 MW;  16596FF2509A9AAA CRC64;
     MSETIHLTEY LFRRLREVGL QAVHGVPGDY NLLMMDYIVP AGLEWVGNCN ELNAGYAADG
     YARVKGIGAL VTTFGVGELS AINAIAGSYA EMAPVIHIVG TPKRAMQTRG AKLHHSVCSG
     KPSDFTMFAE MYSKITAAQE NLWDASTAPA QIDRLIRECI IQSRPVYLQV PADMVTETVP
     AAALSRPLDL TPPSNDPETE QEICNIIVER ISNAKQPFIL IDAGTSRYGL VSEADKLVRI
     TGFPTATTPF GKGIPDETLP NFHGIYASVG EGTYLPYVES SDLIINIGPV HSNVNTSCFT
     TIPNSRVSIV FDQTSITIDG EVYNVFPKGV LKRVLDHLQD AMLSFWPYPN LPDPRSTLKH
     ISRATSAGAL TQDIFFKRMS YFFRPGDIIL TETGTASNGG RDFVFPQNVS MINSGVWLSI
     GYMLGAAQGV ALAQRNMVSQ GRTILFIGDG SFQVTAQELS TIIRKKLSAI IFMINNDGYT
     IERLIHGMDA DYNDIAMWRY LDSPSYFGAP SDDSYPVFTA RVSTWGELDG VLSRESFQRG
     PGLRMVELMM GVSDCTETLR LFLKMYAARK E
//
DBGET integrated database retrieval system