ID   PDC2_TOBAC              Reviewed;         614 AA.
AC   P51846;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Pyruvate decarboxylase 2;
DE            Short=NtPDC2;
DE            EC=4.1.1.1;
GN   Name=PDC2;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Samsun; TISSUE=Pollen;
RX   PubMed=7647304; DOI=10.1007/bf00021197;
RA   Bucher M., Brander K., Sbicego S., Mandel T., Kuhlemeier C.;
RT   "Aerobic fermentation in tobacco pollen.";
RL   Plant Mol. Biol. 28:739-750(1995).
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   -!- TISSUE SPECIFICITY: Pollen.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; X81855; CAA57448.1; -; mRNA.
DR   PIR; S57821; S57821.
DR   RefSeq; NP_001312861.1; NM_001325932.1.
DR   AlphaFoldDB; P51846; -.
DR   SMR; P51846; -.
DR   STRING; 4097.P51846; -.
DR   ProMEX; P51846; -.
DR   GeneID; 107814772; -.
DR   KEGG; nta:107814772; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..614
FT                   /note="Pyruvate decarboxylase 2"
FT                   /id="PRO_0000090778"
FT   REGION          415..523
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         518
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         524
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   614 AA;  67056 MW;  D2E23B505D8B3421 CRC64;
     MDGSVAKGTS CIQDSQSSSV IANTDATLGR HLARRLVEIG IQDVFSVPGD FNLTLLDHLI
     AEPRLKNIGC CNELNAGYAA DGYARARGVG ACVVTFTVGG LSVLNAIAGA YSENLPVICI
     VGGPNTNDYG TNRILHHTIG LPDFSQELRC FQTVTCYQAV VNNLDDAHEQ IDRAISTALK
     ESKPVYISIS CNLPAIPHPT FSRDPIPFSL SPRLSNKRGL EAAVDAAVTF LSKAVKPVMI
     GGPKLRVAKA CDAFVELADS SGYAMAVMLQ PKGLVAEQHP HFIGTYWGAV GTSYCAEIVE
     SADAYLFAGP IFNDYSSVGY SLLIKKEKSI IVQPDRVVIG NGPAFGCVLM KDFLSELAKK
     IKKNETAYEN YRRIFVPEGT PLKSEPNEPL RVNVLFQHIQ KMLSDETAVI AETGDSWFNC
     QKLKLPEGCG YVTNNSLSAW YPFYLQTLEE KSSCCRYEFQ MQYGSIGWSV GATLGYAQSV
     PKKRVISCIG DGSFQVTAQD VSTMIRCEQK NIIFLINNGG YTIEVEIHDG PYNVIKNWNY
     TGLVDAIHNG EGNCWTMKVR TEEELTEAIA TATGEKKDCL CFIEVIVHKD DTSKELLEWG
     SRVCSANGRP PNPQ