ID   PDC_ASPPA               Reviewed;         577 AA.
AC   P51844;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Pyruvate decarboxylase;
DE            EC=4.1.1.1;
GN   Name=pdcA; Synonyms=pdc;
OS   Aspergillus parasiticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / Su-1 / SRRC 143;
RX   PubMed=8181725; DOI=10.1111/j.1574-6968.1994.tb06766.x;
RA   Sanchis V., Vinas I., Roberts I.N., Jeenes D.J., Watson A.J., Archer D.B.;
RT   "A pyruvate decarboxylase gene from Aspergillus parasiticus.";
RL   FEMS Microbiol. Lett. 117:207-210(1994).
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   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000250};
CC       Note=Binds 1 metal ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; U00967; AAA20440.1; -; Genomic_DNA.
DR   AlphaFoldDB; P51844; -.
DR   SMR; P51844; -.
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   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR43452; PTHR43452; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Thiamine pyrophosphate.
FT   CHAIN           1..577
FT                   /note="Pyruvate decarboxylase"
FT                   /id="PRO_0000090760"
FT   REGION          388..482
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         450
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         477
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         479
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         483
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   577 AA;  64071 MW;  32146A17FC930156 CRC64;
     MEGETLPLAQ YLFKRLLQLG VDSIFGVPGD YNLTLLDHVV PSGLKWVGNC NELNAGYAAD
     GYSRIKDIGA VVTTFGVGEL SAINAIAGAY AEKAPVVHIV GTPMRASQES RALIHHTFND
     GDYQRFDAIQ EHVTVAQVSL SDHRTAPSEI DRILLQCLLH SRPVRIAIPV DMVPVLVPVA
     GLSSKIQIPP AVRQPQAEEA ALNAVLKRIY SSKKPMILVD GETRSFGMLQ RVNHFIQTIG
     WPTFTSGFGK GLVDETLPNV YGVCTLHQKA FVDSCDLVLV FGPHFSNTNS YNYFLKPADE
     KSVLFSPNSI QVNKDVFRDL PVGYFIEQLT QQLDISRIPT HKHDLVHPSL RTLPEVSPTD
     LVTQTGGFWK RFSPFLRTGD IILGETGTPG YGVNDFILPP QTRLFKPATW LSIGYMLPAA
     LGASHAQRDL VASDQYHSLS NPRTILFIGD GSFQMTVQEL STIIHQKLNV IIFLINNDGY
     TIERCIHGRN QAYNDVAPWR YLKAAEFFGA DQDGEYKAST WEVRTWADLD RVLNDSQLAD
     GKGLRMVEVF MERLDAPDVL MGLLNNQVLR ENAQSRL