(data stored in ACNUC13479 zone)

SWISSPROT: 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   07-JUN-2017, entry version 101.
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; 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;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
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   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: A 2-oxo acid = an aldehyde + CO(2).
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
CC       roots, flowers and siliques. {ECO:0000269|PubMed:12805625}.
CC   -!- INDUCTION: By abscisic acid (ABA), salt and osmotic stress. Not
CC       induced by anoxia. {ECO:0000269|PubMed:12805625}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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   UniGene; At.33904; -.
DR   ProteinModelPortal; Q9M040; -.
DR   SMR; Q9M040; -.
DR   STRING; 3702.AT5G01320.1; -.
DR   PaxDb; Q9M040; -.
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   eggNOG; COG3961; LUCA.
DR   HOGENOM; HOG000061335; -.
DR   InParanoid; Q9M040; -.
DR   KO; K01568; -.
DR   OMA; CKPTTGD; -.
DR   OrthoDB; EOG093605YM; -.
DR   PhylomeDB; Q9M040; -.
DR   BioCyc; ARA:AT5G01320-MONOMER; -.
DR   BRENDA; 4.1.1.1; 399.
DR   PRO; PR:Q9M040; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q9M040; AT.
DR   GO; GO:0005622; C:intracellular; 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   Gene3D; 3.40.50.1220; -; 1.
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; Q9M040.
DR   SWISS-2DPAGE; Q9M040.
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Pyruvate; Reference proteome; Stress response; Thiamine pyrophosphate.
FT   CHAIN         1    603       Pyruvate decarboxylase 4.
FT                                /FTId=PRO_0000422315.
FT   REGION      430    512       Thiamine pyrophosphate binding.
FT                                {ECO:0000250}.
FT   METAL       480    480       Magnesium. {ECO:0000250}.
FT   METAL       507    507       Magnesium. {ECO:0000250}.
FT   METAL       509    509       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING      65     65       Substrate. {ECO:0000250}.
FT   BINDING     152    152       Substrate. {ECO:0000250}.
FT   BINDING     513    513       Substrate. {ECO:0000250}.
FT   CONFLICT    512    512       I -> T (in Ref. 3; AAO42252).
FT                                {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
//

If you have problems or comments...

PBIL Back to PBIL home page