ID   CHMU_ENTAG              Reviewed;         181 AA.
AC   P42517;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Monofunctional chorismate mutase;
DE            EC=5.4.99.5;
DE   AltName: Full=CM-F;
DE   Flags: Precursor;
GN   Name=aroQ;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-34, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 33243 / DSM 4609 / NCPPB 2971;
RX   PubMed=8335631; DOI=10.1128/jb.175.15.4729-4737.1993;
RA   Xia T., Song J., Zhao G., Aldrich H., Jensen R.A.;
RT   "The aroQ-encoded monofunctional chorismate mutase (CM-F) protein is a
RT   periplasmic enzyme in Erwinia herbicola.";
RL   J. Bacteriol. 175:4729-4737(1993).
RN   [2]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 15277;
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. May sequester with cyclohexadienyl dehydratase and an
CC       aromatic aminotransferase to form phenylalanine or phenylpyruvate.
CC       {ECO:0000269|PubMed:8335631}.
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:8335631};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=169 uM for chorismate (at 32 degrees Celsius)
CC         {ECO:0000269|PubMed:11532214};
CC         Note=kcat is 9.7 sec(-1) for chorismate.;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8335631}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8335631}.
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DR   EMBL; M95628; AAA73360.1; -; Genomic_DNA.
DR   PIR; A40607; A40607.
DR   AlphaFoldDB; P42517; -.
DR   SMR; P42517; -.
DR   STRING; 549.BW31_01830; -.
DR   eggNOG; COG1605; Bacteria.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic 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   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Direct protein sequencing; Isomerase; Periplasm;
KW   Phenylalanine biosynthesis; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:8335631"
FT   CHAIN           21..181
FT                   /note="Monofunctional chorismate mutase"
FT                   /id="PRO_0000023925"
FT   DOMAIN          21..102
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  20299 MW;  5F8F77C0D1E2542E CRC64;
     MTHFVAIFFS SLFMCSNVFA GSVSSVSLGS LSSALNERMQ VMKAVAGYKA LHHLPIEDLP
     REQVVLDHML QNAQQAGLEP HSVEPFVHAL MNASKTIQYR YRADWLSSPD SAVPVRDLTE
     TRQQIQQLDT QLLTAISQRL MTGAFSQEDK EFLMSHLTAP HLSESDKNSL FASLSRIQRQ
     H