CM2_ARATH
ID CM2_ARATH Reviewed; 265 AA.
AC Q9S7H4;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chorismate mutase 2 {ECO:0000303|Ref.2};
DE Short=AtCM2 {ECO:0000303|Ref.2};
DE EC=5.4.99.5 {ECO:0000269|PubMed:10564818, ECO:0000269|PubMed:25160622, ECO:0000269|PubMed:8953244};
DE AltName: Full=CM-2 {ECO:0000303|Ref.2};
GN Name=CM2 {ECO:0000303|Ref.2};
GN OrderedLocusNames=At5g10870 {ECO:0000312|Araport:AT5G10870};
GN ORFNames=T30N20.140 {ECO:0000312|EMBL:CAB96842.1};
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], CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, INDUCTION, AND PATHWAY.
RX PubMed=8953244; DOI=10.1046/j.1365-313x.1996.10050815.x;
RA Eberhard J., Ehrler T.T., Epple P., Felix G., Raesecke H.R., Amrhein N.,
RA Schmid J.;
RT "Cytosolic and plastidic chorismate mutase isozymes from Arabidopsis
RT thaliana: molecular characterization and enzymatic properties.";
RL Plant J. 10:815-821(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Kuhn R., Vogt E., Schmid J., Amrhein N., Schaller A.;
RT "Expression analysis of Arabidopsis thaliana genes for plastidic (CM1) and
RT cytosolic (CM2) chorismate mutases.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION, AND PATHWAY.
RX PubMed=10564818; DOI=10.1016/s0378-1119(99)00423-0;
RA Mobley E.M., Kunkel B.N., Keith B.;
RT "Identification, characterization and comparative analysis of a novel
RT chorismate mutase gene in Arabidopsis thaliana.";
RL Gene 240:115-123(1999).
RN [7]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, HOMODIMERIZATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25160622; DOI=10.1074/jbc.m114.591123;
RA Westfall C.S., Xu A., Jez J.M.;
RT "Structural evolution of differential amino acid effector regulation in
RT plant chorismate mutases.";
RL J. Biol. Chem. 289:28619-28628(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000269|PubMed:10564818, ECO:0000269|PubMed:25160622,
CC ECO:0000269|PubMed:8953244};
CC -!- ACTIVITY REGULATION: No allosteric regulation.
CC {ECO:0000269|PubMed:10564818, ECO:0000269|PubMed:25160622,
CC ECO:0000269|PubMed:8953244}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for chorismate (at pH 8) {ECO:0000269|PubMed:25160622};
CC KM=0.23 mM for chorismate {ECO:0000269|PubMed:10564818};
CC Note=kcat is 38.7 sec(-1) with chorismate as substrate (at pH 8).
CC {ECO:0000269|PubMed:25160622};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000269|PubMed:10564818,
CC ECO:0000269|PubMed:8953244}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25160622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:B4FUP5}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, cauline leaves and
CC flowers, and at lower levels in rosette leaves and siliques.
CC {ECO:0000269|PubMed:8953244}.
CC -!- INDUCTION: Transiently down-regulated by wounding. Not induced by
CC bacterial elicitor or bacterial and fungal pathogens.
CC {ECO:0000269|PubMed:10564818, ECO:0000269|PubMed:8953244}.
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DR EMBL; L47355; AAD48922.1; -; mRNA.
DR EMBL; AJ242648; CAB54519.1; -; Genomic_DNA.
DR EMBL; AL365234; CAB96842.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91604.1; -; Genomic_DNA.
DR EMBL; AY065238; AAL38714.1; -; mRNA.
DR EMBL; AY133840; AAM91774.1; -; mRNA.
DR PIR; T50796; T50796.
DR RefSeq; NP_196648.1; NM_121125.3.
DR AlphaFoldDB; Q9S7H4; -.
DR SMR; Q9S7H4; -.
DR STRING; 3702.AT5G10870.1; -.
DR PaxDb; Q9S7H4; -.
DR PRIDE; Q9S7H4; -.
DR ProteomicsDB; 240897; -.
DR EnsemblPlants; AT5G10870.1; AT5G10870.1; AT5G10870.
DR GeneID; 830954; -.
DR Gramene; AT5G10870.1; AT5G10870.1; AT5G10870.
DR KEGG; ath:AT5G10870; -.
DR Araport; AT5G10870; -.
DR TAIR; locus:2183755; AT5G10870.
DR eggNOG; KOG0795; Eukaryota.
DR HOGENOM; CLU_057757_0_0_1; -.
DR InParanoid; Q9S7H4; -.
DR OMA; NINEKIW; -.
DR OrthoDB; 1087630at2759; -.
DR PhylomeDB; Q9S7H4; -.
DR BioCyc; ARA:AT5G10870-MON; -.
DR BioCyc; MetaCyc:AT5G10870-MON; -.
DR BRENDA; 5.4.99.5; 399.
DR SABIO-RK; Q9S7H4; -.
DR UniPathway; UPA00120; UER00203.
DR PRO; PR:Q9S7H4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7H4; baseline and differential.
DR Genevisible; Q9S7H4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:1901747; P:prephenate(2-) biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.590.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008238; Chorismate_mutase_AroQ_euk.
DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic.
DR PANTHER; PTHR21145; PTHR21145; 1.
DR PIRSF; PIRSF017318; Chor_mut_AroQ_eu; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01802; CM_pl-yst; 1.
DR PROSITE; PS51169; CHORISMATE_MUT_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Isomerase; Reference proteome.
FT CHAIN 1..265
FT /note="Chorismate mutase 2"
FT /id="PRO_0000422192"
FT DOMAIN 10..265
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
SQ SEQUENCE 265 AA; 30491 MW; 8F2616AE7482FA00 CRC64;
MARVFESDSG SGCSNVLSLD LIRESLIRQE DTIVFSLIER AKFPLNSPAF EESRCLDSGS
FSSLTEFFVR ETEIIQAKVG RYEYPEENPF FLENIPHSVF PTHKYPSALH PKALSVNINK
QIWDIYFKEL LPLFVKPGDD GNYPSTAASD LACLQALSRR IHYGKFVAEV KFRDAPQDYE
PAIRAQDREA LMKLLTFEKV EEMVKKRVQK KAETFGQEVK FNSGYGDESK KKYKVDPLLA
SRIYGEWLIP LTKLVEVEYL LRRLD
