ID   SCMU_MYCTO              Reviewed;         199 AA.
AC   P9WIB8; L0T9J1; O07746; Q7D7U7;
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=Secreted chorismate mutase {ECO:0000250|UniProtKB:P9WIB9};
DE            Short=CM {ECO:0000250|UniProtKB:P9WIB9};
DE            EC=5.4.99.5 {ECO:0000250|UniProtKB:P9WIB9};
DE   AltName: Full=*MtCM {ECO:0000250|UniProtKB:P9WIB9};
DE   Flags: Precursor;
GN   OrderedLocusNames=MT1933;
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. May play some role in the pathogenicity.
CC       {ECO:0000250|UniProtKB:P9WIB9}.
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:P9WIB9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC         Evidence={ECO:0000250|UniProtKB:P9WIB9};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P9WIB9}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WIB9}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WIB9}.
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DR   EMBL; AE000516; AAK46206.1; -; Genomic_DNA.
DR   PIR; B70516; B70516.
DR   RefSeq; WP_003899064.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIB8; -.
DR   SMR; P9WIB8; -.
DR   EnsemblBacteria; AAK46206; AAK46206; MT1933.
DR   GeneID; 45425858; -.
DR   KEGG; mtc:MT1933; -.
DR   PATRIC; fig|83331.31.peg.2081; -.
DR   HOGENOM; CLU_090313_1_0_11; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
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; 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   3: Inferred from homology;
KW   Disulfide bond; Isomerase; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   CHAIN           34..199
FT                   /note="Secreted chorismate mutase"
FT                   /id="PRO_0000428034"
FT   DOMAIN          34..113
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   BINDING         72..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   BINDING         105..109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT   DISULFID        160..193
FT                   /evidence="ECO:0000250|UniProtKB:P9WIB9"
SQ   SEQUENCE   199 AA;  21945 MW;  BC5DFB776FC3FA1E CRC64;
     MLTRPREIYL ATAVSIGILL SLIAPLGPPL ARADGTSQLA ELVDAAAERL EVADPVAAFK
     WRAQLPIEDS GRVEQQLAKL GEDARSQHID PDYVTRVFDD QIRATEAIEY SRFSDWKLNP
     ASAPPEPPDL SASRSAIDSL NNRMLSQIWS HWSLLSAPSC AAQLDRAKRD IVRSRHLDSL
     YQRALTTATQ SYCQALPPA