PDC2_ORYSI
ID PDC2_ORYSI Reviewed; 606 AA.
AC A2XFI3; P51848;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Pyruvate decarboxylase 2;
DE Short=PDC;
DE EC=4.1.1.1;
GN Name=PDC2; ORFNames=OsI_010826;
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 / MRNA].
RC STRAIN=cv. IR54; TISSUE=Callus;
RA Huq M.E., Hossain M.A., Hodges T.K.;
RT "Cloning and sequencing of a cDNA encoding pyruvate decarboxylase 2 gene
RT from rice.";
RL (er) Plant Gene Register PGR95-072(1995).
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=AAA90948.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA90948.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAB40530.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB40530.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; U27350; AAA90948.1; ALT_SEQ; mRNA.
DR EMBL; U38199; AAB40530.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A2XFI3; -.
DR SMR; A2XFI3; -.
DR STRING; 39946.A2XFI3; -.
DR EnsemblPlants; BGIOSGA010938-TA; BGIOSGA010938-PA; BGIOSGA010938.
DR Gramene; BGIOSGA010938-TA; BGIOSGA010938-PA; BGIOSGA010938.
DR HOGENOM; CLU_013748_0_2_1; -.
DR OMA; EQRYNDI; -.
DR BRENDA; 4.1.1.1; 4460.
DR SABIO-RK; A2XFI3; -.
DR Proteomes; UP000007015; Chromosome 3.
DR ExpressionAtlas; A2XFI3; differential.
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..606
FT /note="Pyruvate decarboxylase 2"
FT /id="PRO_0000303668"
FT REGION 433..515
FT /note="Thiamine pyrophosphate binding"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 606 AA; 64847 MW; A43F1E7DBB6B46B6 CRC64;
METHIGSVDG AAAAADNGAV GCPASAVGCP MTSARPAPVS AGEASLGRHL ARRLVQVGVS
DVFAVPGDFN LTLLDHLIAE PGLRLVGCCN ELNAGYAADG YARARGVGAC AVTFTVGGLS
VLNAIAGAYS ENLPVICIAG GPNSNDYGTN RILHHTIGLP DFSQELRCFQ TVTCHQAVVT
NLEDAHEQID TAIATALRES KPVYLSISCN LPGLPHPTFS RDPVPFFLAP RLSNKMGLEA
AVEATVEFLN KAVKPVLVGG PKLRVAKAGK AFVDLVDASG YAYAVMPSAK GLVPETHPHF
IGTYWGAVST AFCAEIVESA DAYLFAGPIF NDYSSVGYSF LLKKDKAIIV QPERVIVGNG
PAFGCVMMKE FLSELAKRVN KNTTAYENYK RIFVPEGQPL ESEPNEPLRV NVLFKHVQKM
LNSDSAVIAE TGDSWFNCQK LKLPEGCGYE FQMQYGSIGW SVGALLGYAQ GAKDKRVIAC
IGDGSFQVTA QDVSTMIRCA QNSIIFLINN GGYTIEVEIH DGPYNVIKNW NYTGLVDAIH
NGEGKCWTSK VKCEEELTEA IGMALGEKKD CLCFIEVIAH KDDTSKELLE WGSRVSAANS
RPPNPQ
