CORI3_ARATH
ID CORI3_ARATH Reviewed; 422 AA.
AC Q9SUR6; Q0WN47;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cystine lyase CORI3 {ECO:0000303|PubMed:12525491};
DE EC=4.4.1.35 {ECO:0000269|PubMed:12525491};
DE AltName: Full=Protein CORONATINE INDUCED 3 {ECO:0000303|PubMed:11500565};
DE AltName: Full=Protein JASMONATE RESPONSIVE 2 {ECO:0000303|PubMed:9342878};
GN Name=CORI3 {ECO:0000303|PubMed:11500565};
GN Synonyms=JR2 {ECO:0000303|PubMed:9342878};
GN OrderedLocusNames=At4g23600 {ECO:0000312|Araport:AT4G23600};
GN ORFNames=F9D16.70 {ECO:0000312|EMBL:CAA23026.1};
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 [MRNA] (ISOFORM 1), SUBUNIT, AND INDUCTION.
RX PubMed=11500565; DOI=10.1104/pp.126.4.1678;
RA Lopukhina A., Dettenberg M., Weiler E.W., Hollander-Czytko H.;
RT "Cloning and characterization of a coronatine-regulated tyrosine
RT aminotransferase from Arabidopsis.";
RL Plant Physiol. 126:1678-1687(2001).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=9342878; DOI=10.1104/pp.115.2.817;
RA Titarenko E., Rojo E., Leon J., Sanchez-Serrano J.J.;
RT "Jasmonic acid-dependent and -independent signaling pathways control wound-
RT induced gene activation in Arabidopsis thaliana.";
RL Plant Physiol. 115:817-826(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=12525491; DOI=10.1074/jbc.m212207200;
RA Jones P.R., Manabe T., Awazuhara M., Saito K.;
RT "A new member of plant CS-lyases. A cystine lyase from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 278:10291-10296(2003).
RN [8]
RP INDUCTION BY CORONATINE.
RX PubMed=16008101; DOI=10.1016/j.jplph.2005.04.019;
RA Hollaender-Czytko H., Grabowski J., Sandorf I., Weckermann K., Weiler E.W.;
RT "Tocopherol content and activities of tyrosine aminotransferase and cystine
RT lyase in Arabidopsis under stress conditions.";
RL J. Plant Physiol. 162:767-770(2005).
RN [9]
RP INDUCTION BY WOUNDING.
RX PubMed=18247047; DOI=10.1007/s00425-008-0694-4;
RA Suza W.P., Staswick P.E.;
RT "The role of JAR1 in Jasmonoyl-L: -isoleucine production during Arabidopsis
RT wound response.";
RL Planta 227:1221-1232(2008).
RN [10]
RP INDUCTION.
RX PubMed=19304739; DOI=10.1093/pcp/pcp044;
RA Kawamura Y., Takenaka S., Hase S., Kubota M., Ichinose Y., Kanayama Y.,
RA Nakaho K., Klessig D.F., Takahashi H.;
RT "Enhanced defense responses in Arabidopsis induced by the cell wall protein
RT fractions from Pythium oligandrum require SGT1, RAR1, NPR1 and JAR1.";
RL Plant Cell Physiol. 50:924-934(2009).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=21559970; DOI=10.1007/s00299-011-1080-4;
RA Tsuwamoto R., Harada T.;
RT "The Arabidopsis CORI3 promoter contains two cis-acting regulatory regions
RT required for transcriptional activity in companion cells.";
RL Plant Cell Rep. 30:1723-1733(2011).
CC -!- FUNCTION: Possesses cystine lyase activity in vitro. Does not possess
CC tyrosine aminotransferase, alanine aminotransferase, aspartate
CC aminotransferase and tryptophan aminotransferase activities.
CC {ECO:0000269|PubMed:12525491}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cystine = NH4(+) + pyruvate + S-sulfanyl-L-cysteine;
CC Xref=Rhea:RHEA:24927, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:35491, ChEBI:CHEBI:58591; EC=4.4.1.35;
CC Evidence={ECO:0000269|PubMed:12525491};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12525491};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:11500565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SUR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SUR6-2; Sequence=VSP_041764;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, sepals, pistils, flower
CC buds, phloem companion cells and vascular tissues of petiole, leaf,
CC filament and fruit. {ECO:0000269|PubMed:21559970}.
CC -!- INDUCTION: Induced by jasmonate (PubMed:11500565, PubMed:9342878).
CC Induced by coronatine (PubMed:11500565, PubMed:16008101). Induced by
CC 12-oxo-phytodienoic acid (OPDA) (PubMed:11500565). Induced by wounding
CC (PubMed:11500565, PubMed:9342878, PubMed:18247047). Induced by abscisic
CC acid (ABA) (PubMed:9342878). Induced by the cell wall elicitin from the
CC non-pathogenic biocontrol agent Pythium oligandrum (PubMed:19304739).
CC {ECO:0000269|PubMed:11500565, ECO:0000269|PubMed:16008101,
CC ECO:0000269|PubMed:18247047, ECO:0000269|PubMed:19304739,
CC ECO:0000269|PubMed:9342878}.
CC -!- MISCELLANEOUS: Induction by wounding requires COI1.
CC {ECO:0000269|PubMed:9342878}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: CORI3 was initially isolated by Lopukhina et al
CC (PMID:11500565) as tyrosine aminotransferase (TAT). The authors also
CC measured a TAT activity in vitro, even though relatively weak. Jones et
CC al (PMID:12525491) showed that CORI3 possesses cystine lyase (CL)
CC activity, but lacks TAT activity in vitro. In addition, CL activity is
CC not inhibited by saturation of L-tyrosine in the medium. As CORI3
CC should bind L-tyrosine to catalyze TAT activity, this excludes a TAT
CC activity for CORI3. Jones et al. made the statment that TAT activity
CC resulted probably from residual native TAT-catalyzing proteins present
CC in the purified preparations employed by Loupokhina et al.
CC {ECO:0000305|PubMed:11500565, ECO:0000305|PubMed:12525491}.
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DR EMBL; AF268090; AAK82963.1; -; mRNA.
DR EMBL; AL035394; CAA23026.1; -; Genomic_DNA.
DR EMBL; AL161559; CAB79315.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84781.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84782.1; -; Genomic_DNA.
DR EMBL; AY099811; AAM20662.1; -; mRNA.
DR EMBL; BT000307; AAN15626.1; -; mRNA.
DR EMBL; AK229608; BAF01453.1; -; mRNA.
DR PIR; T05592; T05592.
DR RefSeq; NP_194091.1; NM_118491.3. [Q9SUR6-1]
DR RefSeq; NP_849430.1; NM_179099.3. [Q9SUR6-2]
DR AlphaFoldDB; Q9SUR6; -.
DR SMR; Q9SUR6; -.
DR BioGRID; 13749; 1.
DR STRING; 3702.AT4G23600.1; -.
DR PaxDb; Q9SUR6; -.
DR PRIDE; Q9SUR6; -.
DR ProteomicsDB; 241110; -. [Q9SUR6-1]
DR EnsemblPlants; AT4G23600.1; AT4G23600.1; AT4G23600. [Q9SUR6-1]
DR EnsemblPlants; AT4G23600.2; AT4G23600.2; AT4G23600. [Q9SUR6-2]
DR GeneID; 828460; -.
DR Gramene; AT4G23600.1; AT4G23600.1; AT4G23600. [Q9SUR6-1]
DR Gramene; AT4G23600.2; AT4G23600.2; AT4G23600. [Q9SUR6-2]
DR KEGG; ath:AT4G23600; -.
DR Araport; AT4G23600; -.
DR TAIR; locus:2128459; AT4G23600.
DR eggNOG; KOG0259; Eukaryota.
DR InParanoid; Q9SUR6; -.
DR OMA; FCERHSA; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q9SUR6; -.
DR BioCyc; ARA:AT4G23600-MON; -.
DR BioCyc; MetaCyc:AT4G23600-MON; -.
DR BRENDA; 4.4.1.35; 399.
DR PRO; PR:Q9SUR6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUR6; baseline and differential.
DR Genevisible; Q9SUR6; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IDA:TAIR.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; NAS:TAIR.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEP:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0010188; P:response to microbial phytotoxin; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..422
FT /note="Cystine lyase CORI3"
FT /id="PRO_0000412729"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041764"
SQ SEQUENCE 422 AA; 47039 MW; 7B817B042BF18036 CRC64;
MATLKCIDWQ FSGSEAAKDA AAASLGSYTS ALYALCDPHG KPILPPRNEI LETSNTAEKA
VVKAVLYGSG NAYAPSLGLA AAKSAVAEYL NQGLPKKLTA DDVFMTLGCK QAIELAVDIL
AKPKANVLLP SPGFPWDLVR SIYKNLEVRH YNFLPEKNFE IDFDSVRALV DENTFAIFII
NPHNPNGNTY SEAHLKQLAE LAKELKIMVV SDEVFRWTLF GSNPFVPMGK FSSIVPVVTL
GSISKGWKVP GWRTGWLTLH DLDGVFRNTK VLQAAQDFLQ INNNPPTVIQ AAIPDILEKT
PQEFFDKRQS FLKDKVEFGY SKLKYIPSLT CYMKPEACTF LWTELDLSSF VDIEDDQDFC
NKLAKEENLV VLPGIAFSQK NWLRHSIDME TPVLEDALER LKSFCDRHSN KKAPLKDVNG
VK
