(data stored in ACNUC13479 zone)

SWISSPROT: 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   08-MAY-2019, entry version 112.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Hayashizaki Y., 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
RT   anoxia 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}.
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   SMR; Q9M039; -.
DR   STRING; 3702.AT5G01330.1; -.
DR   PaxDb; Q9M039; -.
DR   PRIDE; Q9M039; -.
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   eggNOG; COG3961; LUCA.
DR   HOGENOM; HOG000061335; -.
DR   InParanoid; Q9M039; -.
DR   KO; K01568; -.
DR   OMA; IFWGQVS; -.
DR   OrthoDB; 560466at2759; -.
DR   PhylomeDB; Q9M039; -.
DR   BioCyc; ARA:AT5G01330-MONOMER; -.
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   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;
DR   PRODOM; Q9M039.
DR   SWISS-2DPAGE; Q9M039.
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Pyruvate; Reference proteome; Stress response; Thiamine pyrophosphate.
FT   CHAIN         1    592       Pyruvate decarboxylase 3.
FT                                /FTId=PRO_0000422314.
FT   REGION      419    501       Thiamine pyrophosphate binding.
FT                                {ECO:0000250}.
FT   METAL       469    469       Magnesium. {ECO:0000250}.
FT   METAL       496    496       Magnesium. {ECO:0000250}.
FT   METAL       498    498       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING      54     54       Substrate. {ECO:0000250}.
FT   BINDING     141    141       Substrate. {ECO:0000250}.
FT   BINDING     502    502       Substrate. {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
//

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