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PDC2_ORYSJ
ID   PDC2_ORYSJ              Reviewed;         605 AA.
AC   Q10MW3; P51848;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Pyruvate decarboxylase 2;
DE            Short=PDC;
DE            EC=4.1.1.1;
GN   Name=PDC2; OrderedLocusNames=Os03g0293500, LOC_Os03g18220;
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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; DP000009; ABF95411.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11725.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS83688.1; -; Genomic_DNA.
DR   EMBL; AK101594; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015631876.1; XM_015776390.1.
DR   AlphaFoldDB; Q10MW3; -.
DR   SMR; Q10MW3; -.
DR   STRING; 4530.OS03T0293500-02; -.
DR   PaxDb; Q10MW3; -.
DR   PRIDE; Q10MW3; -.
DR   EnsemblPlants; Os03t0293500-02; Os03t0293500-02; Os03g0293500.
DR   GeneID; 4332519; -.
DR   Gramene; Os03t0293500-02; Os03t0293500-02; Os03g0293500.
DR   KEGG; osa:4332519; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   InParanoid; Q10MW3; -.
DR   OMA; TTHGVGE; -.
DR   OrthoDB; 560466at2759; -.
DR   PlantReactome; R-OSA-1119267; Phenylalanine degradation III.
DR   PlantReactome; R-OSA-1119460; Isoleucine biosynthesis from threonine.
DR   PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR   PlantReactome; R-OSA-1119600; Valine biosynthesis.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q10MW3; baseline and differential.
DR   Genevisible; Q10MW3; OS.
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..605
FT                   /note="Pyruvate decarboxylase 2"
FT                   /id="PRO_0000090780"
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   605 AA;  64719 MW;  3D664983C10D88A9 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 IGMALGEKDC LCFIEVIAHK DDTSKELLEW GSRVSAANSR
     PPNPQ
 
 
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