CM1_ARATH
ID CM1_ARATH Reviewed; 340 AA.
AC P42738; Q29Q24; Q9LS75; Q9SUJ5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Chorismate mutase 1, chloroplastic {ECO:0000303|Ref.1};
DE Short=AtCM1 {ECO:0000303|Ref.1};
DE EC=5.4.99.5 {ECO:0000269|PubMed:10564818, ECO:0000269|PubMed:25160622, ECO:0000269|PubMed:8953244};
DE AltName: Full=CM-1 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=CM1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At3g29200 {ECO:0000312|Araport:AT3G29200};
GN ORFNames=MXO21.4 {ECO:0000312|EMBL:BAB01816.1};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-340.
RX PubMed=8224252; DOI=10.1016/0014-5793(93)81718-f;
RA Eberhard J., Raesecke H.-R., Schmid J., Amrhein N.;
RT "Cloning and expression in yeast of a higher plant chorismate mutase.
RT Molecular cloning, sequencing of the cDNA and characterization of the
RT Arabidopsis thaliana enzyme expressed in yeast.";
RL FEBS Lett. 334:233-236(1993).
RN [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, 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 [7]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-66, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER HIS-65, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9] {ECO:0007744|PDB:4PPU, ECO:0007744|PDB:4PPV}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 65-340 IN COMPLEXES WITH
RP L-PHENYLALANINE AND L-TYROSINE, HOMODIMERIZATION, ACTIVITY REGULATION,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-79; HIS-145; GLY-149; GLY-213 AND
RP VAL-217, 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 ECO:0000269|PubMed:8953244};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by tyrosine and
CC phenylalanine. Activated by tryptophan. {ECO:0000269|PubMed:10564818,
CC ECO:0000269|PubMed:25160622, ECO:0000269|PubMed:8953244}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=550 uM for chorismate (at pH 8) {ECO:0000269|PubMed:25160622};
CC KM=2.9 mM for chorismate {ECO:0000269|PubMed:10564818};
CC Vmax=29 umol/min/mg enzyme with chorismate as substrate (apoenzyme at
CC pH 8) {ECO:0000269|PubMed:25160622};
CC Vmax=55 umol/min/mg enzyme with chorismate as substrate (in the
CC presence of tryptophan at pH 8) {ECO:0000269|PubMed:25160622};
CC Vmax=1.4 umol/min/mg enzyme with chorismate as substrate (in the
CC presence of tyrosine at pH 8) {ECO:0000269|PubMed:25160622};
CC Vmax=1.2 umol/min/mg enzyme with chorismate as substrate (in the
CC presence of phenylalanine at pH 8) {ECO:0000269|PubMed:25160622};
CC Note=kcat is 16.1 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: Plastid, chloroplast
CC {ECO:0000305|PubMed:22223895}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, rosette leaves, stems,
CC cauline leaves, flowers and siliques. {ECO:0000269|PubMed:10564818}.
CC -!- INDUCTION: By wounding, P.syringae, bacterial elicitor and the fungal
CC pathogens F.oxysporum and A.raphani. {ECO:0000269|PubMed:10564818,
CC ECO:0000269|PubMed:8953244}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01816.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA81286.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB54518.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ242647; CAB54518.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB026657; BAB01816.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE77552.1; -; Genomic_DNA.
DR EMBL; BT024732; ABD59070.1; -; mRNA.
DR EMBL; Z26519; CAA81286.1; ALT_INIT; mRNA.
DR PIR; S38958; S38958.
DR RefSeq; NP_566846.1; NM_113844.4.
DR PDB; 4PPU; X-ray; 2.30 A; A=65-340.
DR PDB; 4PPV; X-ray; 2.45 A; A=65-340.
DR PDBsum; 4PPU; -.
DR PDBsum; 4PPV; -.
DR AlphaFoldDB; P42738; -.
DR SMR; P42738; -.
DR STRING; 3702.AT3G29200.1; -.
DR iPTMnet; P42738; -.
DR PaxDb; P42738; -.
DR PRIDE; P42738; -.
DR ProteomicsDB; 240896; -.
DR EnsemblPlants; AT3G29200.1; AT3G29200.1; AT3G29200.
DR GeneID; 822573; -.
DR Gramene; AT3G29200.1; AT3G29200.1; AT3G29200.
DR KEGG; ath:AT3G29200; -.
DR Araport; AT3G29200; -.
DR TAIR; locus:2094832; AT3G29200.
DR eggNOG; KOG0795; Eukaryota.
DR HOGENOM; CLU_057757_0_0_1; -.
DR InParanoid; P42738; -.
DR OMA; FLDWALM; -.
DR OrthoDB; 1087630at2759; -.
DR BioCyc; ARA:AT3G29200-MON; -.
DR BioCyc; MetaCyc:AT3G29200-MON; -.
DR BRENDA; 5.4.99.5; 399.
DR SABIO-RK; P42738; -.
DR UniPathway; UPA00120; UER00203.
DR PRO; PR:P42738; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P42738; baseline and differential.
DR Genevisible; P42738; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:TAIR.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; ISS:TAIR.
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 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 3D-structure; Acetylation; Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Isomerase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 66..340
FT /note="Chorismate mutase 1, chloroplastic"
FT /id="PRO_0000023926"
FT DOMAIN 79..340
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 79
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:25160622,
FT ECO:0007744|PDB:4PPV"
FT BINDING 150
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:25160622,
FT ECO:0007744|PDB:4PPU"
FT BINDING 211..214
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:25160622,
FT ECO:0007744|PDB:4PPV"
FT BINDING 211..214
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000269|PubMed:25160622,
FT ECO:0007744|PDB:4PPU"
FT SITE 149
FT /note="Controls amino acid effector specificity"
FT /evidence="ECO:0000269|PubMed:25160622"
FT MOD_RES 66
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 79
FT /note="R->K: Enhanced activity with slightly reduced
FT allosteric inhibition by tyrosine and phenylalanine, but
FT normal activation by tryptophan."
FT /evidence="ECO:0000269|PubMed:25160622"
FT MUTAGEN 145
FT /note="H->Q: Strongly reduced activity, but almost normal
FT allosteric regulation by tyrosine, phenylalanine and
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:25160622"
FT MUTAGEN 149
FT /note="G->D,A: Increased activation by tryptophan but
FT abolished allosteric repression by tyrosine and
FT phenylalanine."
FT /evidence="ECO:0000269|PubMed:25160622"
FT MUTAGEN 213
FT /note="G->P,A: Normal activity and abolished allosteric
FT regulation by tyrosine, phenylalanine and tryptophan."
FT /evidence="ECO:0000269|PubMed:25160622"
FT MUTAGEN 217
FT /note="V->T: Enhanced activity, but strong allosteric
FT inhibition by tyrosine and phenylalanine, and normal
FT activation by tryptophan."
FT /evidence="ECO:0000269|PubMed:25160622"
FT CONFLICT 259
FT /note="A -> R (in Ref. 1; CAA81286)"
FT /evidence="ECO:0000305"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 91..109
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:4PPU"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 212..231
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 267..284
FT /evidence="ECO:0007829|PDB:4PPU"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:4PPU"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:4PPU"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:4PPU"
SQ SEQUENCE 340 AA; 38239 MW; 28037093334B71AE CRC64;
MEASLLMRSS CCSSAIGGFF DHRRELSTST PISTLLPLPS TKSSFSVRCS LPQPSKPRSG
TSSVHAVMTL AGSLTGKKRV DESESLTLEG IRNSLIRQED SIIFGLLERA KYCYNADTYD
PTAFDMDGFN GSLVEYMVKG TEKLHAKVGR FKSPDEHPFF PDDLPEPMLP PLQYPKVLHF
AADSININKK IWNMYFRDLV PRLVKKGDDG NYGSTAVCDA ICLQCLSKRI HYGKFVAEAK
FQASPEAYES AIKAQDKDAL MDMLTFPTVE DAIKKRVEMK TRTYGQEVKV GMEEKEEEEE
EGNESHVYKI SPILVGDLYG DWIMPLTKEV QVEYLLRRLD
