ID   CHMU_SALTM              Reviewed;         181 AA.
AC   Q93LJ4; Q7CQP9;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Monofunctional chorismate mutase {ECO:0000250|UniProtKB:P42517, ECO:0000312|EMBL:AAK91555.1};
DE            EC=5.4.99.5 {ECO:0000269|PubMed:11532214};
DE   Flags: Precursor;
GN   Name=aroQ {ECO:0000303|PubMed:11532214};
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK91555.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-30, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=LT2 {ECO:0000312|EMBL:AAK91555.1};
RX   PubMed=11532214; DOI=10.1186/gb-2001-2-8-research0030;
RA   Calhoun D.H., Bonner C.A., Gu W., Xie G., Jensen R.A.;
RT   "The emerging periplasm-localized subclass of AroQ chorismate mutases,
RT   exemplified by those from Salmonella typhimurium and Pseudomonas
RT   aeruginosa.";
RL   Genome Biol. 2:RESEARCH0030.1-RESEARCH0030.16(2001).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate. {ECO:0000250|UniProtKB:P0A9J8}.
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:11532214};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=142 uM for chorismate (at 32 degrees Celsius)
CC         {ECO:0000269|PubMed:11532214};
CC         Note=kcat is 8.9 sec(-1) for chorismate.
CC         {ECO:0000269|PubMed:11532214};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P42517}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11532214}.
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DR   EMBL; AY039113; AAK91555.1; -; Genomic_DNA.
DR   RefSeq; WP_000617985.1; NZ_WXYU01000003.1.
DR   AlphaFoldDB; Q93LJ4; -.
DR   SMR; Q93LJ4; -.
DR   eggNOG; COG1605; Bacteria.
DR   OMA; RSAPDCP; -.
DR   UniPathway; UPA00120; UER00203.
DR   GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR   GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR   GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR008240; Chorismate_mutase_periplasmic.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   Pfam; PF01817; CM_2; 1.
DR   PIRSF; PIRSF026640; Peripl_chor_mut; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01806; CM_mono2; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Periplasm; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:11532214"
FT   CHAIN           21..181
FT                   /note="Monofunctional chorismate mutase"
FT                   /evidence="ECO:0000269|PubMed:11532214"
FT                   /id="PRO_0000419449"
FT   DOMAIN          21..102
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515,
FT                   ECO:0000305"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
SQ   SEQUENCE   181 AA;  20582 MW;  17E5F7952C0B1BF8 CRC64;
     MIRHIAIFLC SLLMCSTTFA DSVTSVSLGA LLTALNERML LMKDVAAYKM KHHLPIEDFT
     REQNVFAEAE EEAKNNGLDP HSITPFIRSL MDASKAIQYR YLAQWRTGSE PSFPIQTLSV
     TRQRIRQLDN QMLIIISQRL MVGAFSHDDM VWLRAQFNAP NLNESDISNV LAALSLVRRA
     R