PDC1_ARATH
ID PDC1_ARATH Reviewed; 607 AA.
AC O82647; Q96535;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pyruvate decarboxylase 1;
DE Short=AtPDC1;
DE EC=4.1.1.1;
GN Name=PDC1; OrderedLocusNames=At4g33070; ORFNames=F4I10.4;
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 [GENOMIC DNA].
RC STRAIN=cv. C24;
RA Dolferus R., Peacock W.J., Dennis E.S.;
RT "Two pyruvate decarboxylase genes from Arabidopsis.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
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 -!- FUNCTION: May play a role in ethanolic fermentation during anoxia.
CC {ECO:0000269|PubMed:12805625}.
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: Highly expressed in seeds, and at lower levels in
CC roots and siliques. {ECO:0000269|PubMed:12805625}.
CC -!- INDUCTION: By anoxia and abscisic acid (ABA).
CC {ECO:0000269|PubMed:12805625}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plant roots are more sensitive to anoxia.
CC {ECO:0000269|PubMed:12805625}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; U71121; AAB16854.1; -; Genomic_DNA.
DR EMBL; AL031804; CAA21216.1; -; Genomic_DNA.
DR EMBL; AL161582; CAB80024.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86169.1; -; Genomic_DNA.
DR EMBL; AY070036; AAL49793.1; -; mRNA.
DR EMBL; AY122926; AAM67459.1; -; mRNA.
DR PIR; T05315; T05315.
DR RefSeq; NP_195033.1; NM_119461.4.
DR AlphaFoldDB; O82647; -.
DR SMR; O82647; -.
DR BioGRID; 14729; 9.
DR STRING; 3702.AT4G33070.1; -.
DR PaxDb; O82647; -.
DR PRIDE; O82647; -.
DR ProteomicsDB; 236289; -.
DR EnsemblPlants; AT4G33070.1; AT4G33070.1; AT4G33070.
DR GeneID; 829444; -.
DR Gramene; AT4G33070.1; AT4G33070.1; AT4G33070.
DR KEGG; ath:AT4G33070; -.
DR Araport; AT4G33070; -.
DR TAIR; locus:2123827; AT4G33070.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; O82647; -.
DR OMA; PMRASQE; -.
DR OrthoDB; 560466at2759; -.
DR PhylomeDB; O82647; -.
DR BioCyc; ARA:AT4G33070-MON; -.
DR BRENDA; 4.1.1.1; 399.
DR PRO; PR:O82647; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O82647; baseline and differential.
DR Genevisible; O82647; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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 GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0034059; P:response to anoxia; IMP:UniProtKB.
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..607
FT /note="Pyruvate decarboxylase 1"
FT /id="PRO_0000422312"
FT REGION 434..516
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 220
FT /note="F -> Y (in Ref. 1; AAB16854)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="P -> Q (in Ref. 1; AAB16854)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="I -> IA (in Ref. 1; AAB16854)"
FT /evidence="ECO:0000305"
FT CONFLICT 447..449
FT /note="GCG -> R (in Ref. 1; AAB16854)"
FT /evidence="ECO:0000305"
FT CONFLICT 583..584
FT /note="DD -> GE (in Ref. 1; AAB16854)"
FT /evidence="ECO:0000305"
FT CONFLICT 594..603
FT /note="SRVSAANSRP -> HASLLLTAVL (in Ref. 1; AAB16854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66212 MW; 9AB439C9112FC80A CRC64;
MDTKIGSIDD CKPTNGDVCS PTNGTVATIH NSVPSSAITI NYCDATLGRH LARRLVQAGV
TDVFSVPGDF NLTLLDHLMA EPDLNLIGCC NELNAGYAAD GYARSRGVGA CVVTFTVGGL
SVLNAIAGAY SENLPLICIV GGPNSNDYGT NRILHHTIGL PDFSQELRCF QTVTCYQAVV
NNLDDAHEQI DKAISTALKE SKPVYISVSC NLAAIPHHTF SRDPVPFSLA PRLSNKMGLE
AAVEATLEFL NKAVKPVMVG GPKLRVAKAC DAFVELADAS GYALAMMPSA KGFVPEHHPH
FIGTYWGAVS TPFCSEIVES ADAYIFAGPI FNDYSSVGYS LLLKKEKAIV VQPDRITVAN
GPTFGCILMS DFFRELSKRV KRNETAYENY HRIFVPEGKP LKCESREPLR VNTMFQHIQK
MLSSETAVIA ETGDSWFNCQ KLKLPKGCGY EFQMQYGSIG WSVGATLGYA QASPEKRVLA
FIGDGSFQVT VQDISTMLRN GQKTIIFLIN NGGYTIEVEI HDGPYNVIKN WNYTGLVDAI
HNGEGNCWTA KVRYEEELVE AITTATTEKK DCLCFIEVIL HKDDTSKELL EWGSRVSAAN
SRPPNPQ
