CM2_PETHY
ID CM2_PETHY Reviewed; 263 AA.
AC D2CSU5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Chorismate mutase 2 {ECO:0000303|PubMed:19811620};
DE Short=PhCM2 {ECO:0000303|PubMed:19811620};
DE EC=5.4.99.5 {ECO:0000255|PROSITE-ProRule:PRU00516, ECO:0000269|PubMed:19811620};
GN Name=CM2 {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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, PATHWAY, AND ACTIVITY REGULATION.
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).
CC -!- FUNCTION: Mediates the conversion of chorismate to prephenate.
CC {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: No allosteric regulation.
CC {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: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:B4FUP5}.
CC -!- TISSUE SPECIFICITY: Expressed in root, stem, stigma, anther, leaf,
CC petal tube, petal limb and sepal tissues with highest levels in petal
CC tubes and stems. {ECO:0000269|PubMed:19811620}.
CC -!- DEVELOPMENTAL STAGE: Expressed at similar levels throughout all
CC flowering stages but accumulates in senescing flowers.
CC {ECO:0000269|PubMed:19811620}.
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DR EMBL; EU751617; ACI41890.1; -; mRNA.
DR AlphaFoldDB; D2CSU5; -.
DR SMR; D2CSU5; -.
DR BRENDA; 5.4.99.5; 4700.
DR UniPathway; UPA00120; UER00203.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 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.
FT CHAIN 1..263
FT /note="Chorismate mutase 2"
FT /id="PRO_0000451506"
FT DOMAIN 3..256
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
SQ SEQUENCE 263 AA; 30287 MW; 5AF6F68F1C401A59 CRC64;
MACGDYDDKL SLDLIRDSLI RQEDTIIFNL IERIKFPINS TLYKKPSSWF PDFTGSLFQY
LFQETEALQS KVGRYLSPEE NPFFPDNLPA SIVPPSKCPP VLHPVAESIN INEKILDVYL
NQLLPLFCTE ADEGNYATTA ACDIQLLQAI SRRIHYGKFV AEVKFRDCSD EYTPLILAQQ
DRDALMKLLT FEVVEEMVKK RVAKKAMIFG QEVTLVDNAK EVKCKVDPLL VSRLYDEWIM
PLTKHVQVEY LLRRLDQNKL TSI
