PDC1_TOBAC
ID PDC1_TOBAC Reviewed; 418 AA.
AC P51845;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Pyruvate decarboxylase 1;
DE Short=PDC;
DE EC=4.1.1.1;
DE Flags: Fragment;
GN Name=PDC1;
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=Leaf;
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: Leaves.
CC -!- INDUCTION: Anaerobically.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; X81854; CAA57447.1; -; mRNA.
DR PIR; S57820; S57820.
DR AlphaFoldDB; P51845; -.
DR SMR; P51845; -.
DR STRING; 4097.P51845; -.
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 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..>418
FT /note="Pyruvate decarboxylase 1"
FT /id="PRO_0000090777"
FT REGION 337..418
FT /note="Thiamine pyrophosphate binding"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 418
SQ SEQUENCE 418 AA; 45011 MW; 7C3C33DAA9FFD804 CRC64;
AADGYARARG VGACVVTFTV GGLSVLNAIA GAYSENLPLI CIVGGPNSND YGTNRILHHT
IGLQDFSQEP RCFQTVTCYR AVVNNLEDAH ELIDTAVSTA LKESKPVYIS IGCNLPGIPH
PTFSREPVPF ALSPRLSNMM GLEAAVEAAA EFLNKAVKPV LVGGPKMRVA KASDAFVELS
DACGYAVAVM PSAKGLFPEH HSHFIGTYWG AVSTAFCAEI VESADAYLFA GPIFNDYSSV
GYSLLLKKEK AIIVQPDRVT IGNGPAFGCV LMRDFLAALA KRLKHNPTAF ENYHRIYVPE
GHPLKCEPKE ALRVNVLFQH IQNMLSGDSV VIAETGDSWF NCQKLKLPKG CGYEFQMQYG
SIGWSVGATL GYAQAAPEKR VIACIGDGSF QVTAQDISTM LRCGQRTIIF LINNGGYT
