CM1_PETHY
ID CM1_PETHY Reviewed; 324 AA.
AC D2CSU4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Chorismate mutase 1, chloroplastic {ECO:0000303|PubMed:19811620};
DE Short=PhCM1 {ECO:0000303|PubMed:19811620};
DE EC=5.4.99.5 {ECO:0000255|PROSITE-ProRule:PRU00516, ECO:0000269|PubMed:19811620};
DE Flags: Precursor;
GN Name=CM1 {ECO:0000303|PubMed:19811620};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=cv. Mitchell;
RX PubMed=19811620; DOI=10.1111/j.1365-313x.2009.04042.x;
RA Colquhoun T.A., Schimmel B.C., Kim J.Y., Reinhardt D., Cline K.,
RA Clark D.G.;
RT "A petunia chorismate mutase specialized for the production of floral
RT volatiles.";
RL Plant J. 61:145-155(2010).
RN [2]
RP INDUCTION BY EOBI.
RC STRAIN=cv. W115;
RX PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT regulates scent production by activating ODO1 and structural scent-related
RT genes in petunia.";
RL Plant Cell 24:5089-5105(2012).
CC -!- FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid
CC (FVBPs) biosynthetic pathway (PubMed:19811620). Mediates the conversion
CC of chorismate to prephenate, thus coupling metabolites from the
CC shikimate pathway to the synthesis of FVBPs in the corolla
CC (PubMed:19811620). {ECO:0000269|PubMed:19811620}.
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:0000255|PROSITE-ProRule:PRU00516,
CC ECO:0000269|PubMed:19811620};
CC -!- ACTIVITY REGULATION: Allosterically activated by tryptophan but not by
CC tyrosine and phenylalanine. {ECO:0000269|PubMed:19811620}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000269|PubMed:19811620}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B4FNK8}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19811620}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in petal tubes and petal limbs,
CC and, to a lower extent, in stigmas, anthers, sepals, roots, stems and
CC leaves. {ECO:0000269|PubMed:19811620}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during flower development with highest
CC levels in open flowers, at anthesis, and fades out as flowers are
CC senescing. {ECO:0000269|PubMed:19811620}.
CC -!- INDUCTION: Triggered by EOBI in flowers. {ECO:0000269|PubMed:23275577}.
CC -!- DISRUPTION PHENOTYPE: Reduced emission of floral volatile
CC benzenoid/phenylpropanoid (FVBP) compounds associated with a strongly
CC impaired chorismate mutase activity in corolla tissues.
CC {ECO:0000269|PubMed:19811620}.
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DR EMBL; EU751616; ACI41889.1; -; mRNA.
DR AlphaFoldDB; D2CSU4; -.
DR SMR; D2CSU4; -.
DR BRENDA; 5.4.99.5; 4700.
DR UniPathway; UPA00120; UER00203.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP: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 Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Isomerase; Plastid;
KW Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..324
FT /note="Chorismate mutase 1, chloroplastic"
FT /id="PRO_0000451505"
FT DOMAIN 70..324
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 70
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 141
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 202..205
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
FT BINDING 202..205
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P42738"
SQ SEQUENCE 324 AA; 36946 MW; EE706D0664B026EC CRC64;
METQLLRFPS HTITSSITTN SSRNTTPFLP HKKWSHFVKF QLVNSSSSIK HGIRPLQASA
TSLGLGNKNR VDETESYTLD GIRHSLIRQE DSIIFSLVER AQYCYNAETY DPDVFAMDGF
HGSLVEYIVR ETEKLHATVG RYKSPDEHPF FPKVLPEPVL PPMQYPKVLH PIADSININV
KIWEMYFENL LPRLVKEGDD GNYGSTAVCD TICVQALSKR IHYGKFVAEA KYRASPEVYN
AAIRAQDRNG LMDLLTYPAV EEAIKRRVEI KTRTYGQELH INGPENGGDP VYKIKPSLVA
ELYGDWIMPL TKEVQVQYLL RRLD
