ID   CHMU_MYCTO              Reviewed;         105 AA.
AC   P9WIC0; L0T5D6; P64767; P71562;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Intracellular chorismate mutase {ECO:0000250|UniProtKB:P9WIC1};
DE            Short=CM {ECO:0000250|UniProtKB:P9WIC1};
DE            EC=5.4.99.5 {ECO:0000250|UniProtKB:P9WIC1};
GN   OrderedLocusNames=MT0975;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate. Probably involved in the aromatic amino acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WIC1}.
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:0000250|UniProtKB:P9WIC1};
CC   -!- ACTIVITY REGULATION: The formation of the complex with AroG activates
CC       the chorismate mutase activity. {ECO:0000250|UniProtKB:P9WIC1}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P9WIC1}.
CC   -!- SUBUNIT: Homodimer. Interacts with AroG.
CC       {ECO:0000250|UniProtKB:P9WIC1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WIC1}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45223.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45223.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70716; B70716.
DR   RefSeq; WP_003404838.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIC0; -.
DR   SMR; P9WIC0; -.
DR   EnsemblBacteria; AAK45223; AAK45223; MT0975.
DR   GeneID; 45424917; -.
DR   KEGG; mtc:MT0975; -.
DR   PATRIC; fig|83331.31.peg.1046; -.
DR   HOGENOM; CLU_1271163_0_0_11; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR010958; Chorismate_mutase_highGC-bac.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   Pfam; PF01817; CM_2; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01808; CM_M_hiGC-arch; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase.
FT   CHAIN           1..105
FT                   /note="Intracellular chorismate mutase"
FT                   /id="PRO_0000428033"
FT   DOMAIN          23..105
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   BINDING         61
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT   BINDING         70
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT   BINDING         74
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT   SITE            61
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT   SITE            101
FT                   /note="Important for activation via AroG"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT   SITE            102
FT                   /note="Important for activation via AroG"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT   SITE            103
FT                   /note="Important for activation via AroG"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC1"
SQ   SEQUENCE   105 AA;  11771 MW;  6A387E4A53CC9F6D CRC64;
     MRPEPPHHEN AELAAMNLEM LESQPVPEID TLREEIDRLD AEILALVKRR AEVSKAIGKA
     RMASGGTRLV HSREMKVIER YSELGPDGKD LAILLLRLGR GRLGH