CMU_ERYQU
ID CMU_ERYQU Reviewed; 262 AA.
AC A0A5B8NIM2;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Chorismate mutase {ECO:0000303|PubMed:33010586};
DE EC=5.4.99.5 {ECO:0000269|PubMed:33010586};
DE AltName: Full=EqCMU {ECO:0000303|PubMed:33010586};
GN Name=CMU {ECO:0000303|PubMed:33010586};
OS Erysiphe quercicola (Hevea powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=425177;
RN [1] {ECO:0000312|EMBL:QDZ38301.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PATHWAY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF ARG-162 AND LYS-173.
RC STRAIN=HO-73 {ECO:0000303|PubMed:33010586};
RX PubMed=33010586; DOI=10.1016/j.micres.2020.126599;
RA He Q., Liu Y., Liang P., Liao X., Li X., Li X., Shi D., Liu W., Lin C.,
RA Zheng F., Miao W.;
RT "A novel chorismate mutase from Erysiphe quercicola performs dual functions
RT of synthesizing amino acids and inhibiting plant salicylic acid
RT synthesis.";
RL Microbiol. Res. 242:126599-126599(2020).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate (PubMed:33010586). May function both as an effector during
CC plant infection and in the fungal tyrosine and phenylalanine
CC biosynthesis pathways (PubMed:33010586). During infection it channels
CC chorismate into the phenylpropanoid pathway, thereby decreasing the
CC synthesis of the plant immune signal salicylic acid (Probable). Within
CC fungal cells, it acts at the first branch point in the aromatic amino
CC acid pathway where it steers biosynthesis towards phenylalanine and
CC tyrosine, and away from tryptophan (Probable).
CC {ECO:0000269|PubMed:33010586, ECO:0000305|PubMed:33010586}.
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:33010586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000269|PubMed:33010586};
CC -!- ACTIVITY REGULATION: Contrary to classical chorismate mutases, is not
CC subject to allosteric regulation by tryptophan or tyrosine
CC (PubMed:33010586). Also not regulated by phenylalanine
CC (PubMed:33010586). {ECO:0000269|PubMed:33010586}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:33010586}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:33010586}. Secreted
CC {ECO:0000305|PubMed:33010586}. Host cytoplasm
CC {ECO:0000305|PubMed:33010586}. Note=Appears to be secreted despite an
CC apparent lack of a secretory signal. {ECO:0000305|PubMed:33010586}.
CC -!- DEVELOPMENTAL STAGE: Present during infection; expression is higher in
CC hausturia than epiphytic mycelia. {ECO:0000269|PubMed:33010586}.
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DR EMBL; MK391402; QDZ38301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8NIM2; -.
DR SMR; A0A5B8NIM2; -.
DR UniPathway; UPA00120; UER00203.
DR GO; GO:0005737; C:cytoplasm; IGI:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IGI:UniProtKB.
DR GO; GO:0030430; C:host cell cytoplasm; IC:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0046417; P:chorismate metabolic process; IGI:UniProtKB.
DR GO; GO:0140502; P:effector-mediated suppression of host salicylic acid-mediated innate immune signalling; IDA:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IGI:UniProtKB.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IGI: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 Host cytoplasm; Isomerase; Phenylalanine biosynthesis; Secreted;
KW Tyrosine biosynthesis; Virulence.
FT CHAIN 1..262
FT /note="Chorismate mutase"
FT /id="PRO_0000452011"
FT DOMAIN 7..261
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT REGION 1..100
FT /note="May contain the secretory signal"
FT /evidence="ECO:0000305|PubMed:33010586"
FT MUTAGEN 162
FT /note="R->A: Abolishes catalytic activity; when associated
FT with A-173."
FT /evidence="ECO:0000269|PubMed:33010586"
FT MUTAGEN 173
FT /note="K->A: Abolishes catalytic activity; when associated
FT with A-162."
FT /evidence="ECO:0000269|PubMed:33010586"
SQ SEQUENCE 262 AA; 30282 MW; ECA2ECEEF9558D35 CRC64;
MDAAVDLLDP SKALNLKHIR QQLIRMEDTI TFQLIERVQF PLNRTVYEPG AVKIPNSNLS
FLDWTLRERE KTDSLIRRYQ SPDEHPFFPD ALLKPILQPL IYPKILHRNN INLNDKIKKY
FTDQVLPSIC HDFGREDRGE QAENYGSTVT ADIQCLQTLS RRIHFGKWVA ESKYIDDPQG
FAKLIKAGDR QAIGKAITKP AVELQVLERI RLKSRTYSTD PCESDDPEPK INVDAVVAMY
RDCVIPLTKE VEIDYLMQRL SD
