PDC3_ARATH
ID PDC3_ARATH Reviewed; 592 AA.
AC Q9M039;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pyruvate decarboxylase 3;
DE Short=AtPDC3;
DE EC=4.1.1.1;
GN Name=PDC3; OrderedLocusNames=At5g01330; ORFNames=T10O8.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12805625; DOI=10.1104/pp.102.016907;
RA Kuersteiner O., Dupuis I., Kuhlemeier C.;
RT "The pyruvate decarboxylase1 gene of Arabidopsis is required during anoxia
RT but not other environmental stresses.";
RL Plant Physiol. 132:968-978(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 -!- TISSUE SPECIFICITY: Expressed at low levels in roots and shoots.
CC {ECO:0000269|PubMed:12805625}.
CC -!- INDUCTION: By wounding and paraquat. Not induced by anoxia.
CC {ECO:0000269|PubMed:12805625}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AL161746; CAB81916.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90328.1; -; Genomic_DNA.
DR EMBL; BT006455; AAP21263.1; -; mRNA.
DR EMBL; AK227701; BAE99688.1; -; mRNA.
DR PIR; T48155; T48155.
DR RefSeq; NP_195753.1; NM_120211.3.
DR AlphaFoldDB; Q9M039; -.
DR SMR; Q9M039; -.
DR BioGRID; 16690; 7.
DR STRING; 3702.AT5G01330.1; -.
DR PaxDb; Q9M039; -.
DR PRIDE; Q9M039; -.
DR ProteomicsDB; 236718; -.
DR EnsemblPlants; AT5G01330.1; AT5G01330.1; AT5G01330.
DR GeneID; 831414; -.
DR Gramene; AT5G01330.1; AT5G01330.1; AT5G01330.
DR KEGG; ath:AT5G01330; -.
DR Araport; AT5G01330; -.
DR TAIR; locus:2179147; AT5G01330.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q9M039; -.
DR OMA; TTHGVGE; -.
DR OrthoDB; 560466at2759; -.
DR PhylomeDB; Q9M039; -.
DR BioCyc; ARA:AT5G01330-MON; -.
DR BRENDA; 4.1.1.1; 399.
DR PRO; PR:Q9M039; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M039; baseline and differential.
DR Genevisible; Q9M039; AT.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Pyruvate;
KW Reference proteome; Stress response; Thiamine pyrophosphate.
FT CHAIN 1..592
FT /note="Pyruvate decarboxylase 3"
FT /id="PRO_0000422314"
FT REGION 419..501
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 592 AA; 64482 MW; 8C46D5AE2C272F36 CRC64;
MDVRSLPSNG VATIQDSAPT AATILGSSAA TLGRHLSRRL VQAGVTDIFT VPGDFNLSLL
DQLIANPELN NIGCCNELNA GYAADGYARS RGVGACVVTF TVGGLSVLNA IAGAYSENLP
VICIVGGPNS NDFGTNRILH HTIGLPDFSQ ELRCFQTVTC YQAVVNHLED AHEQIDKAIA
TALRESKPVY ISISCNLAAI PHPTFASYPV PFDLTPRLSN KDCLEAAVEA TLEFLNKAVK
PVMVGGPKLR VAKARDAFVE LADASGYPVA VMPSAKGFVP ENHPHFIGTY WGAVSTLFCS
EIVESADAYI FAGPIFNDYS SVGYSLLLKK EKAIIVHPDS VVVANGPTFG CVRMSEFFRE
LAKRVKPNKT AYENYHRIFV PEGKPLKCKP REPLRINAMF QHIQKMLSNE TAVIAETGDS
WFNCQKLKLP KGCGYEFQMQ YGSIGWSVGA TLGYAQATPE KRVLSFIGDG SFQVTAQDVS
TMIRNGQKTI IFLINNGGYT IEVEIHDGPY NVIKNWNYTG LVDAIHNGEG KCWTTKVRYE
EELVEAINTA TLEKKDSLCF IEVIVHKDDT SKELLEWGSR VSAANGRPPN PQ
