ID   PDC3_MAIZE              Reviewed;         202 AA.
AC   Q05327;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Pyruvate decarboxylase 3;
DE            Short=PDC;
DE            EC=4.1.1.1;
DE   Flags: Fragment;
GN   Name=PDC3;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Berkeley Fast; TISSUE=Seedling;
RX   PubMed=8102778; DOI=10.1007/bf00277058;
RA   Peschke V.M., Sachs M.M.;
RT   "Multiple pyruvate decarboxylase genes in maize are induced by hypoxia.";
RL   Mol. Gen. Genet. 240:206-212(1993).
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;
CC       Note=Binds 1 metal ion per subunit.;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC       Note=Binds 1 thiamine pyrophosphate per subunit.;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Appears in endosperm 15 days post-pollination.
CC   -!- INDUCTION: By hypoxic stress.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; Z21722; CAA79819.1; -; mRNA.
DR   EMBL; D14457; BAA03354.1; -; mRNA.
DR   PIR; S35259; S35259.
DR   AlphaFoldDB; Q05327; -.
DR   SMR; Q05327; -.
DR   STRING; 4577.GRMZM2G087186_P01; -.
DR   PaxDb; Q05327; -.
DR   PRIDE; Q05327; -.
DR   MaizeGDB; 25417; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q05327; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   InterPro; IPR029061; THDP-binding.
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   SUPFAM; SSF52518; SSF52518; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Stress response; Thiamine pyrophosphate.
FT   CHAIN           <1..202
FT                   /note="Pyruvate decarboxylase 3"
FT                   /id="PRO_0000090776"
FT   REGION          30..112
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   202 AA;  22297 MW;  2911A55C59D80AAD CRC64;
     PNEPLRVNVL FKHVQKMLTG DSAVIAETGD SWFNCQKLKL PEGCGYEFQM QYGSIGWSVG
     ALLGYPQGAN HKRVIAFIGD GSFQVTAQDV STILRCEQNS IIFLINNGGY TIEVEIHDGP
     YNVIKNWNYT GFVDAIHNGL GKCWTSKVKS EEDLTAAIET ALGEKDCLCF IEVIAHKDDT
     SKELLEWGSR VSAANSRPPN PQ