PDC1_ORYSI
ID PDC1_ORYSI Reviewed; 605 AA.
AC A2Y5L9; P51847; Q6AUJ9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Pyruvate decarboxylase 1;
DE Short=PDC;
DE EC=4.1.1.1;
GN Name=PDC1; ORFNames=OsI_019612;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. IR54; TISSUE=Callus;
RX PubMed=7991697; DOI=10.1104/pp.106.2.799;
RA Hossain M.A., Hug E., Hodges T.K.;
RT "Sequence of a cDNA from Oryza sativa (L.) encoding the pyruvate
RT decarboxylase 1 gene.";
RL Plant Physiol. 106:799-800(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. IR54; TISSUE=Callus;
RX PubMed=8806407; DOI=10.1007/bf00019464;
RA Hossain M.A., Huq E., Grover A., Dennis E.S., Peacock W.J., Hodges T.K.;
RT "Characterization of pyruvate decarboxylase genes from rice.";
RL Plant Mol. Biol. 31:761-770(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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; U07339; AAA68290.1; -; mRNA.
DR EMBL; U26660; AAC49442.1; -; Genomic_DNA.
DR EMBL; CM000130; EAY98379.1; -; Genomic_DNA.
DR PIR; S71557; S71557.
DR AlphaFoldDB; A2Y5L9; -.
DR SMR; A2Y5L9; -.
DR STRING; 39946.A2Y5L9; -.
DR EnsemblPlants; BGIOSGA020021-TA; BGIOSGA020021-PA; BGIOSGA020021.
DR Gramene; BGIOSGA020021-TA; BGIOSGA020021-PA; BGIOSGA020021.
DR HOGENOM; CLU_013748_0_2_1; -.
DR OMA; YPNVRMK; -.
DR Proteomes; UP000007015; Chromosome 5.
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..605
FT /note="Pyruvate decarboxylase 1"
FT /id="PRO_0000303667"
FT REGION 432..514
FT /note="Thiamine pyrophosphate binding"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 509
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 42
FT /note="G -> R (in Ref. 1; AAA68290 and 2; AAC49442)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="G -> A (in Ref. 1; AAA68290 and 2; AAC49442)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..110
FT /note="RGVGACA -> LVGAF (in Ref. 1; AAA68290 and 2;
FT AAC49442)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="Missing (in Ref. 1; AAA68290 and 2; AAC49442)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> F (in Ref. 1; AAA68290 and 2; AAC49442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 65144 MW; 96DE1D79D243A54D CRC64;
MELALVGNPS NGVAKPSCNS VGSLPVVSSN AVIHPPVTSA AGATLGRHLA RRLVQIGATD
VFAVPGDFNL TLLDYLIAEP GLKLIGCCNE LNAGYAADGY ARARGVGACA VTFTVGGLSV
LNAIAGAYSE NLPVICIVGG PNSNDYGTNR ILHHTIGLPD FSQELRCFQT ITCYQAVINN
LDDAHEQIDT AIATALRESK PVYISVGCNL AGLSHPTFSR EPVPLFISPR LSNKANLEYA
VEAAADFLNK AVKPVMVGGP KIRVAKAKKA FAGIAESSGY PIAVMPSAKG LVPEHHPRFI
GTYWGAVSTT FCAEIVESAD AYLFAGPIFN DYSSVGYSLL LKREKAVIVQ PDRVVVGNGP
AFGCILMTEF LDALAKRLDR NTTAYDNYRR IFIPDREPPN GQPDEPLRVN ILFKHIKEML
SGDTAVIAET GDSWFNCQKL RLPEGCGYEF QMQYGSIGWS VGATLGYAQA AKDKRVISCI
GDGSFQMTAQ DVSTMLRCGQ KSIIFLINNG GYTIEVEIHD GPYNVIKNWD YTGLIDAIHN
SDGNCWTKKV RTEEELIEAI ATATGAKKDC LCFIEIIVHK DDTSKELLEW GSRVSAANSR
PPNPQ
