PDC_HANUV
ID PDC_HANUV Reviewed; 564 AA.
AC P34734;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Pyruvate decarboxylase;
DE EC=4.1.1.1;
GN Name=PDC;
OS Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=29833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate R15;
RX PubMed=7725793; DOI=10.1002/yea.320101207;
RA Holloway P., Subden R.E.;
RT "The nucleotide sequence and initial characterization of pyruvate
RT decarboxylase from the yeast Hanseniaspora uvarum.";
RL Yeast 10:1581-1589(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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P06169};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; U13635; AAA85103.1; -; Genomic_DNA.
DR PIR; S50700; S50700.
DR AlphaFoldDB; P34734; -.
DR SMR; P34734; -.
DR VEuPathDB; FungiDB:AWRI3580_g175; -.
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..564
FT /note="Pyruvate decarboxylase"
FT /id="PRO_0000090764"
FT BINDING 28
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 115
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 390
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 413..415
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 445..446
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 471..476
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 477
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
SQ SEQUENCE 564 AA; 61070 MW; 9B5D3064F72C5BE5 CRC64;
MSEITLGRYV FERIKQVGVN TIFGLPGDFN LSLLDKIYEV EGLRWAASLN ELNAAYAADG
YSRIKGLGVI ITTFGVGELS ALNGIAGAYA EHVGVLHIVG VPSLASQAKQ LLLHHTLGNG
DFDVFHRMSA NISETTAMIT DLAAAPAEID RCIRTAYIAQ RPVYLGLPAN LVDLNVPAKL
LETKIDLALK ANDAEAENEV VETILALVAD AKNPVILSDA CASRHNVKAE VKQLIDATQF
PAFVTPLGKG SIDEKHPRFG GVYVGTLSSP EVKQSVESAD LILSVGALLS DFNTGSFSYS
YQTKNIVEFH SDYIKIKNAS FPGVQMKFVL EKLIAKVGAK IANYSPVPVP AGLPKNAPVA
DSTPLAQEWL WNELGEFLEE GDIVVTETGT SAFGINQTRF PTDAYGISQV LWGSIGYSVG
AMVGATFAAE ELDKAKRVIL FVGDGSLQLT VQEIACLIRW GLKPYIFVLN NNGYTIEKLI
HGPTAQYNMI QNWKQLRYLT NFGATDYEAI PVKTVGEWKK LTADPAFKKN STIRLIEVFL
PEMDAPSSLV AQANLTAAIN AKQD
