PDC3_ORYSI
ID PDC3_ORYSI Reviewed; 587 AA.
AC A2YQ76; P51849; Q84NP9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Pyruvate decarboxylase 3;
DE Short=PDC;
DE EC=4.1.1.1;
GN Name=PDC3; ORFNames=OsI_026469;
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 [GENOMIC DNA].
RC STRAIN=cv. IR54; TISSUE=Callus;
RX PubMed=7846174; DOI=10.1104/pp.106.4.1697;
RA Hossain M.A., McGee J.D., Grover A., Dennis E., Peacock W.J., Hodges T.K.;
RT "Nucleotide sequence of a rice genomic pyruvate decarboxylase gene that
RT lacks introns: a pseudo-gene?";
RL Plant Physiol. 106:1697-1698(1994).
RN [2]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68289.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA68289.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; U07338; AAA68289.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T03252; T03252.
DR AlphaFoldDB; A2YQ76; -.
DR SMR; A2YQ76; -.
DR STRING; 39946.A2YQ76; -.
DR Proteomes; UP000007015; Chromosome 7.
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 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..587
FT /note="Pyruvate decarboxylase 3"
FT /id="PRO_0000303669"
FT REGION 415..496
FT /note="Thiamine pyrophosphate binding"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 587 AA; 62638 MW; 94F41DF24863118C CRC64;
MESNGGGGGS PKEAAVVVPS SGDATLGGHL ARRLVQVGVS DVFAVPGDFN LTLLDHLIAE
PGLRVVGCCN ELNAGYAADG YARARGVGAC AVTFTVGGLS VLNAIGGAYS ENLPLICIVG
GPNSNDYGTN RILHHTIGLP DFSQELRCFQ PLTCYQAVVN NLDDAHDQID RAISTAIRES
KPVYISVSCN LPAVPHPTFS RDPVPYFLSP RLSNQASLHA ALDATLAFLD KAVKPVLVAG
PKLRVAKAGG AFVDLADASG YAVAAMPSAK GLVPETLPRF IGTYWGAVST AFCAEIVESA
DAYLFAGPIF NDYSSVGYSC LLKKEKAVVV QPDRVTVGNG PAFGCVMMRD FLSELAKRVR
KNTTAFDNYK RIFVPEGQLP ECEAGEALRV NVLFKHIQRM IGGAEIGAVM AETGDSWFNC
QKLRLPEGCG YEFQMQYGSI GWSVGALLGY AQAVQKRVVA CIGDGSFQVT AQDVSTMLRC
GQRSIIFLIN NGGYTIEVEI HDGPYNVIKN WDYVGLVNAI HNGEGRCWAT RVRCEEELEA
AIATATGDKA DSLCFIEVVA HKDDTSKELL EWGSRVSAAN SRPPNPQ
