ID   MENF_MYCTO              Reviewed;         372 AA.
AC   P9WFW8; L0TDH4; O05851; Q7D5X1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative isochorismate synthase MenF;
DE            EC=5.4.4.2 {ECO:0000250|UniProtKB:P38051};
DE   AltName: Full=Isochorismate mutase;
GN   Name=menF; Synonyms=entC; OrderedLocusNames=MT3311;
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 conversion of chorismate to isochorismate.
CC       {ECO:0000250|UniProtKB:P38051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC         Evidence={ECO:0000250|UniProtKB:P38051};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P38051};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
CC       {ECO:0000250|UniProtKB:P38051}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000250|UniProtKB:P38051}.
CC   -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47653.1; -; Genomic_DNA.
DR   PIR; H70595; H70595.
DR   RefSeq; WP_003416879.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFW8; -.
DR   SMR; P9WFW8; -.
DR   EnsemblBacteria; AAK47653; AAK47653; MT3311.
DR   KEGG; mtc:MT3311; -.
DR   PATRIC; fig|83331.31.peg.3565; -.
DR   HOGENOM; CLU_006493_8_6_11; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00163.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.120.10; -; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR004561; IsoChor_synthase.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00543; isochor_syn; 1.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Menaquinone biosynthesis; Metal-binding.
FT   CHAIN           1..372
FT                   /note="Putative isochorismate synthase MenF"
FT                   /id="PRO_0000428464"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P38051"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P38051"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P38051"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P38051"
SQ   SEQUENCE   372 AA;  38938 MW;  E2C1480BC281D8F3 CRC64;
     MSAHVATLHP EPPFALCGPR GTLIARGVRT RYCDVRAAQA ALRSGTAPIL LGALPFDVSR
     PAALMVPDGV LRARKLPDWP TGPLPKVRVA AALPPPADYL TRIGRARDLL AAFDGPLHKV
     VLARAVQLTA DAPLDARVLL RRLVVADPTA YGYLVDLTSA GNDDTGAALV GASPELLVAR
     SGNRVMCKPF AGSAPRAADP KLDAANAAAL ASSAKNRHEH QLVVDTMRVA LEPLCEDLTI
     PAQPQLNRTA AVWHLCTAIT GRLRNISTTA IDLALALHPT PAVGGVPTKA ATELIAELEG
     DRGFYAGAVG WCDGRGDGHW VVSIRCAQLS ADRRAALAHA GGGIVAESDP DDELEETTTK
     FATILTALGV EQ