ID   PDC1_PEA                Reviewed;         593 AA.
AC   P51850;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pyruvate decarboxylase 1;
DE            Short=PDC;
DE            EC=4.1.1.1;
GN   Name=PDC1;
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; Z66543; CAA91444.1; -; mRNA.
DR   PIR; S65470; S65470.
DR   AlphaFoldDB; P51850; -.
DR   SMR; P51850; -.
DR   BioCyc; MetaCyc:MON-15104; -.
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   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Thiamine pyrophosphate.
FT   CHAIN           1..593
FT                   /note="Pyruvate decarboxylase 1"
FT                   /id="PRO_0000090782"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..502
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         499
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         503
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   593 AA;  63967 MW;  86058EB51CF366BF CRC64;
     METETETPNG STPCPTSAPS AIPLRPSSCD GTMGRHLARR LVEIGVRDVF SVPGDFNLTL
     LDHLIAEPEL NLVGCCNELN AGYAADGYGR AKGVGACVVT FTVGGLSILN AIAGAYSENL
     PVICIVGGPN SNDYGTNRIL HHTIGLPDFS QELQCFQTIT CFQAVVNNLD DAHELIDTAI
     STALKESKPV YISIGCNLPA IPHPTFARDP VPFFLAPRVS NQAGLEAAVE EAAAFLNKAV
     KPVIVGGPKL RVAKAQKAFM EFAEASGYPI AVMPSGKGLV PENHPHFIGT YWGAVSTSYC
     GEIVESADAY VFVGPIFNDY SSVGYSLLIK KEKSLIVQPN RVTIGNGLSL GWVFMADFLT
     ALAKKVKTNT TAVENYRRIY VPPGIPLKRE KDEPLRVNVL FKHIQALISG DTAVIAETGD
     SWFNCQKLRL PENCGYEFQM QYGSIGWSVG ATLGYAQAAT DKRVIACIGD GSFQVTAQDI
     STMIRCGQRS IIFLINNGGY TIEVEIHDGP YNVIKNWDYT GFVSAIHNGQ GKCWTAKVRT
     EEDLTEAIAT ATGAEKDSLC FIEVFAHKDD TSKELLEWGS RVAAANSRPP NPQ