ID   PDC2_PEA                Reviewed;         405 AA.
AC   P51851;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Pyruvate decarboxylase 2;
DE            Short=PDC;
DE            EC=4.1.1.1;
DE   Flags: Fragment;
GN   Name=PDC2;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Miko;
RX   PubMed=8647075; DOI=10.1111/j.1432-1033.1996.0373k.x;
RA   Muecke U., Wohlfarth T., Fiedler U., Baeumlein H., Ruecknagel K.P.,
RA   Koenig S.;
RT   "Pyruvate decarboxylase from Pisum sativum. Properties, nucleotide and
RT   amino acid sequences.";
RL   Eur. J. Biochem. 237:373-382(1996).
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   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; Z66544; CAA91445.1; -; mRNA.
DR   PIR; S65471; S65471.
DR   AlphaFoldDB; P51851; -.
DR   SMR; P51851; -.
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; 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   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Thiamine pyrophosphate.
FT   CHAIN           <1..405
FT                   /note="Pyruvate decarboxylase 2"
FT                   /id="PRO_0000090783"
FT   REGION          232..314
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   405 AA;  44079 MW;  44DDCE90B38677FB CRC64;
     PVYISIGCNL PAIPHPTFSR DPVPFSLAPK LSNQMGLEAA VEAAAEFLNK AVKPVLVGGP
     KLRVAKASDA FVELADASGY ALAVMPSAKG MVPEHHPHFI GTYWGAVSTA FCAEIVESAD
     AYLFAGPIFN DYSSVGYSLL LKKEKAIIVM PDRVVIANGP AFGCVLMNDF LKALAKRLKH
     NNVAYENYHR IFVPDGTPLK SASKEPLRVN VMFQHIQKML SSETAVIAET GDSWFNCQKL
     KLPEGCGYEF QMQYGSIGWS VGATLGYAQA VPEKRVIACI GDGSFQVTAQ DVSTMLRCGQ
     KTIIFLINNG GYTIEVEIHD GPYNVIKNWN YTGLVDAIHN GEGKCWTTKV FCEEELVEAI
     AKATGPKKDS LCFIEVIVHK DDTSKELLEW GSRVSAANSR PPNPQ