CM3_ARATH
ID CM3_ARATH Reviewed; 316 AA.
AC Q9C544; Q9XF60;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Chorismate mutase 3, chloroplastic {ECO:0000303|PubMed:10564818};
DE Short=AtCM3 {ECO:0000303|PubMed:10564818};
DE EC=5.4.99.5 {ECO:0000269|PubMed:10564818, ECO:0000269|PubMed:25160622};
DE AltName: Full=CM-3 {ECO:0000303|PubMed:10564818};
DE Flags: Precursor;
GN Name=CM3 {ECO:0000303|PubMed:10564818};
GN OrderedLocusNames=At1g69370 {ECO:0000312|Araport:AT1G69370};
GN ORFNames=F10D13.6 {ECO:0000312|EMBL:AAG60103.1},
GN F23O10.5 {ECO:0000312|EMBL:AAG52497.1};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, HOMODIMERIZATION, MUTAGENESIS OF
RP ASP-132, AND 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 -!- FUNCTION: May play a role in chloroplast biogenesis. {ECO:0000305}.
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 -!- ACTIVITY REGULATION: Allosterically inhibited by tyrosine and
CC phenylalanine (PubMed:10564818). According to another report, seems not
CC to be repressed by tyrosine and phenylalanine (PubMed:25160622).
CC Activated by tryptophan, cysteine and histidine (PubMed:10564818,
CC PubMed:25160622). {ECO:0000269|PubMed:10564818,
CC ECO:0000269|PubMed:25160622}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1100 uM for chorismate (at pH 8) {ECO:0000269|PubMed:25160622};
CC KM=0.42 mM for chorismate {ECO:0000269|PubMed:10564818};
CC Note=Does not follow Michaelis-Menten kinetics but displays a
CC positive cooperativity with a Hill coefficient of 2.1 indicating that
CC substrate binding at one active site of the homodimer enhances
CC interaction at the second active site (PubMed:25160622). kcat is 13.0
CC sec(-1) with chorismate as substrate (at pH 8) (PubMed:25160622).
CC {ECO:0000269|PubMed:25160622};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000269|PubMed:10564818}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25160622}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:B4FNK8}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, cauline leaves, flowers
CC and siliques, and at lower levels in rosette leaves.
CC {ECO:0000269|PubMed:10564818}.
CC -!- INDUCTION: Not induced by wounding or bacterial pathogen.
CC {ECO:0000269|PubMed:10564818}.
CC -!- CAUTION: Due to contradictory results, it is uncertain whether tyrosine
CC and phenylalanine act as allosteric inhibitors.
CC {ECO:0000305|PubMed:10564818, ECO:0000305|PubMed:25160622}.
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DR EMBL; AF131219; AAD21624.1; -; mRNA.
DR EMBL; AC018364; AAG52497.1; -; Genomic_DNA.
DR EMBL; AC073178; AAG60103.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34916.1; -; Genomic_DNA.
DR EMBL; AK117860; BAC42501.1; -; mRNA.
DR EMBL; BT005306; AAO63370.1; -; mRNA.
DR RefSeq; NP_177096.1; NM_105604.2.
DR AlphaFoldDB; Q9C544; -.
DR SMR; Q9C544; -.
DR STRING; 3702.AT1G69370.1; -.
DR PaxDb; Q9C544; -.
DR PRIDE; Q9C544; -.
DR ProteomicsDB; 241071; -.
DR EnsemblPlants; AT1G69370.1; AT1G69370.1; AT1G69370.
DR GeneID; 843269; -.
DR Gramene; AT1G69370.1; AT1G69370.1; AT1G69370.
DR KEGG; ath:AT1G69370; -.
DR Araport; AT1G69370; -.
DR TAIR; locus:2007146; AT1G69370.
DR eggNOG; KOG0795; Eukaryota.
DR HOGENOM; CLU_057757_0_0_1; -.
DR InParanoid; Q9C544; -.
DR OMA; LCDTMCL; -.
DR OrthoDB; 1087630at2759; -.
DR PhylomeDB; Q9C544; -.
DR BioCyc; ARA:AT1G69370-MON; -.
DR BioCyc; MetaCyc:AT1G69370-MON; -.
DR BRENDA; 5.4.99.5; 399.
DR SABIO-RK; Q9C544; -.
DR UniPathway; UPA00120; UER00203.
DR PRO; PR:Q9C544; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C544; baseline and differential.
DR Genevisible; Q9C544; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; TAS:TAIR.
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:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
DR GO; GO:1901747; P:prephenate(2-) biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:TAIR.
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 Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Isomerase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..316
FT /note="Chorismate mutase 3, chloroplastic"
FT /id="PRO_0000422193"
FT DOMAIN 62..316
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 62
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 133
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 194..197
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 194..197
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT SITE 132
FT /note="Controls amino acid effector specificity"
FT /evidence="ECO:0000269|PubMed:25160622"
FT MUTAGEN 132
FT /note="D->G: Slightly reduced activation by tryptophan,
FT abolished activation by cysteine and histidine, but
FT increased allosteric repression by tyrosine and
FT phenylalanine."
FT /evidence="ECO:0000269|PubMed:25160622"
FT CONFLICT 215..221
FT /note="FGKFVAE -> LRKFVAD (in Ref. 1; AAD21624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 36570 MW; 46A56482E30987E2 CRC64;
MEAKLLKPAF YNSPNLNLTN SSRLISRLSI WNDKSKVGLS SGSLFLRLSA ASPIRYSRGL
LRVDESEYLK LESIRHSLIR QEDSIIFNLL ERAQYRYNAD TYDEDAFTME GFQGSLVEFM
VRETEKLHAK VDRYKSPDEH PFFPQCLPEP ILPPIQYPQV LHRCAESINI NKKVWNMYFK
HLLPRLVKPG DDGNCGSAAL CDTMCLQILS KRIHFGKFVA EAKFRENPAA YETAIKEQDR
TQLMQLLTYE TVEEVVKKRV EIKARIFGQD ITINDPETEA DPSYKIQPSL VAKLYGERIM
PLTKEVQIEY LLRRLD
