PDC4_ARATH
ID PDC4_ARATH Reviewed; 603 AA.
AC Q9M040; Q84W45;
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 4;
DE Short=AtPDC4;
DE EC=4.1.1.1;
GN Name=PDC4; OrderedLocusNames=At5g01320; ORFNames=T10O8.30;
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] OF 40-603.
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 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 in shoots and at lowe levels in roots,
CC flowers and siliques. {ECO:0000269|PubMed:12805625}.
CC -!- INDUCTION: By abscisic acid (ABA), salt and osmotic stress. Not induced
CC by anoxia. {ECO:0000269|PubMed:12805625}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL161746; CAB81915.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90327.1; -; Genomic_DNA.
DR EMBL; BT004248; AAO42252.1; -; mRNA.
DR PIR; T48154; T48154.
DR RefSeq; NP_195752.1; NM_120210.3.
DR AlphaFoldDB; Q9M040; -.
DR SMR; Q9M040; -.
DR BioGRID; 16145; 7.
DR STRING; 3702.AT5G01320.1; -.
DR PaxDb; Q9M040; -.
DR PRIDE; Q9M040; -.
DR ProteomicsDB; 236379; -.
DR EnsemblPlants; AT5G01320.1; AT5G01320.1; AT5G01320.
DR GeneID; 830867; -.
DR Gramene; AT5G01320.1; AT5G01320.1; AT5G01320.
DR KEGG; ath:AT5G01320; -.
DR Araport; AT5G01320; -.
DR TAIR; locus:2179132; AT5G01320.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q9M040; -.
DR OMA; IFWGQVS; -.
DR OrthoDB; 560466at2759; -.
DR PhylomeDB; Q9M040; -.
DR BioCyc; ARA:AT5G01320-MON; -.
DR BRENDA; 4.1.1.1; 399.
DR PRO; PR:Q9M040; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M040; baseline and differential.
DR Genevisible; Q9M040; 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..603
FT /note="Pyruvate decarboxylase 4"
FT /id="PRO_0000422315"
FT REGION 430..512
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 509
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 512
FT /note="I -> T (in Ref. 3; AAO42252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 65465 MW; 626A5CDAC899417A CRC64;
MDTKIGAIDT CKPTTGDIGS PPSNAVATIQ DSAPITTTSE STLGRHLSRR LVQAGVTDVF
SVPGDFNLTL LDHLIAEPEL NNIGCCNELN AGYAADGYAR SRGVGACVVT FTVGGLSVLN
AIAGAYSENL PVICIVGGPN SNDFGTNRIL HHTIGLPDFS QELRCFQTVT CYQAVVNNLE
DAHEQIDKAI ATALKESKPV YISISCNLAA TPHPTFARDP VPFDLTPRMS NTMGLEAAVE
ATLEFLNKAV KPVMVGGPKL RVAKASEAFL ELADASGYPL AVMPSTKGLV PENHPHFIGT
YWGAVSTPFC SEIVESADAY IFAGPIFNDY SSVGYSLLLK KEKAIIVHPD RVVVANGPTF
GCVLMSDFFR ELAKRVKRNE TAYENYERIF VPEGKPLKCK PGEPLRVNAM FQHIQKMLSS
ETAVIAETGD SWFNCQKLKL PKGCGYEFQM QYGSIGWSVG ATLGYAQATP EKRVLSFIGD
GSFQVTAQDI STMIRNGQKA IIFLINNGGY TIEVEIHDGP YNVIKNWNYT GLVDAIHNGE
GKCWTTKVRY EEELVEAIKT ATTEKKDSLC FIEVIVHKDD TSKELLEWGS RVSAANGRPP
NPQ
