ID PDC2_ARATH Reviewed; 607 AA.
AC Q9FFT4; Q96536;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Pyruvate decarboxylase 2;
DE Short=AtPDC2;
DE EC=4.1.1.1;
GN Name=PDC2; OrderedLocusNames=At5g54960; ORFNames=MBG8.23;
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. Landsberg erecta;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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, shoots, flowers,
CC siliques and seeds. {ECO:0000269|PubMed:12805625}.
CC -!- INDUCTION: By abscisic acid (ABA), salt, osmotic stress, wounding and
CC paraquat. Not induced by anoxia. {ECO:0000269|PubMed:12805625}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX830776; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; U71122; AAB16855.1; -; Genomic_DNA.
DR EMBL; AB005232; BAB08775.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96563.1; -; Genomic_DNA.
DR EMBL; BX830776; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_200307.1; NM_124878.3.
DR AlphaFoldDB; Q9FFT4; -.
DR SMR; Q9FFT4; -.
DR BioGRID; 20831; 9.
DR STRING; 3702.Q9FFT4; -.
DR PaxDb; 3702-AT5G54960-1; -.
DR ProMEX; Q9FFT4; -.
DR ProteomicsDB; 236329; -.
DR EnsemblPlants; AT5G54960.1; AT5G54960.1; AT5G54960.
DR GeneID; 835587; -.
DR Gramene; AT5G54960.1; AT5G54960.1; AT5G54960.
DR KEGG; ath:AT5G54960; -.
DR Araport; AT5G54960; -.
DR TAIR; AT5G54960; PDC2.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q9FFT4; -.
DR OMA; AQEISVM; -.
DR OrthoDB; 1000728at2759; -.
DR PhylomeDB; Q9FFT4; -.
DR BioCyc; ARA:AT5G54960-MONOMER; -.
DR BRENDA; 4.1.1.1; 399.
DR PRO; PR:Q9FFT4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFT4; baseline and differential.
DR Genevisible; Q9FFT4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0001666; P:response to hypoxia; IEP:TAIR.
DR CDD; cd02005; TPP_PDC_IPDC; 1.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF6; PYRUVATE DECARBOXYLASE C186.09-RELATED; 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; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
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 2"
FT /id="PRO_0000422313"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 368
FT /note="L -> F (in Ref. 1; AAB16855)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="T -> P (in Ref. 1; AAB16855)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Q -> H (in Ref. 1; AAB16855)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="A -> P (in Ref. 1; AAB16855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 65818 MW; 541E596A380BACBE CRC64;
MDTKIGSIDA CNPTNHDIGG PPNGGVSTVQ NTSPLHSTTV SPCDATLGRY LARRLVEIGV
TDVFSVPGDF NLTLLDHLIA EPNLKLIGCC NELNAGYAAD GYARSRGVGA CVVTFTVGGL
SVLNAIAGAY SENLPLICIV GGPNSNDYGT NRILHHTIGL PDFTQELRCF QAVTCFQAVI
NNLEEAHELI DTAISTALKE SKPVYISISC NLPAIPLPTF SRHPVPFMLP MKVSNQIGLD
AAVEAAAEFL NKAVKPVLVG GPKMRVAKAA DAFVELADAS GYGLAVMPSA KGQVPEHHKH
FIGTYWGAVS TAFCAEIVES ADAYLFAGPI FNDYSSVGYS LLLKKEKAII VQPDRVTIGN
GPAFGCVLMK DFLSELAKRI KHNNTSYENY HRIYVPEGKP LRDNPNESLR VNVLFQHIQN
MLSSESAVLA ETGDSWFNCQ KLKLPEGCGY EFQMQYGSIG WSVGATLGYA QAMPNRRVIA
CIGDGSFQVT AQDVSTMIRC GQKTIIFLIN NGGYTIEVEI HDGPYNVIKN WNYTAFVEAI
HNGEGKCWTA KVRCEEELVK AINTATNEEK ESFCFIEVIV HKDDTSKELL EWGSRVSAAN
SRPPNPQ
//
