ID   MENF_PASMU              Reviewed;         431 AA.
AC   Q9CPI5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Isochorismate synthase MenF {ECO:0000255|HAMAP-Rule:MF_01935};
DE            EC=5.4.4.2 {ECO:0000255|HAMAP-Rule:MF_01935};
DE   AltName: Full=Isochorismate mutase {ECO:0000255|HAMAP-Rule:MF_01935};
GN   Name=menF {ECO:0000255|HAMAP-Rule:MF_01935}; OrderedLocusNames=PM0053;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the conversion of chorismate to isochorismate.
CC       {ECO:0000255|HAMAP-Rule:MF_01935}.
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:0000255|HAMAP-Rule:MF_01935};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01935};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
CC       {ECO:0000255|HAMAP-Rule:MF_01935}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01935}.
CC   -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01935}.
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DR   EMBL; AE004439; AAK02137.1; -; Genomic_DNA.
DR   RefSeq; WP_005751036.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPI5; -.
DR   SMR; Q9CPI5; -.
DR   STRING; 747.DR93_2025; -.
DR   EnsemblBacteria; AAK02137; AAK02137; PM0053.
DR   KEGG; pmu:PM0053; -.
DR   PATRIC; fig|272843.6.peg.54; -.
DR   HOGENOM; CLU_006493_8_4_6; -.
DR   OMA; TGHGQSI; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00163.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.120.10; -; 1.
DR   HAMAP; MF_01935; MenF; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR004561; IsoChor_synthase.
DR   InterPro; IPR034681; MenF.
DR   InterPro; IPR044250; MenF-like.
DR   PANTHER; PTHR47253; PTHR47253; 1.
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;
KW   Reference proteome.
FT   CHAIN           1..431
FT                   /note="Isochorismate synthase MenF"
FT                   /id="PRO_0000154149"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT   ACT_SITE        233
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT   BINDING         414
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
SQ   SEQUENCE   431 AA;  48727 MW;  DE03AB3C43AE740F CRC64;
     MDNLQSIKAQ FIAQINAYQP EKDRDIVVFQ CNTETTFSLL AWLKAQQYYP QFYLHGRDGA
     TKWASIGQVR QFSDVSAAAH FIQEQQLALL GGLQFYGDAL FVLPRLLLQQ RQDGMTITLF
     IDGKQFEQDK LVALACLSTF EKQTALQTVK QEISLISQKA DQAEWCRWVE QGLQKIKQGE
     LSKIVLANER CFKTAAPLAA TDLLAESEKY NLGCYHFMLA ESEQRAFIGS SPELLYRRHG
     LQLKTEALAG TAFMGEDEQQ NQQQSDWLLH DKKNEYENQL VVDGICQNLQ PFVQQITIEK
     VELKKLRKVQ HLRRRISAQL KAGCGDKDIL LAMHPTAAVA GLPQLEAKQA LRKLENFDRT
     WYAGTLGVMG PAYADFCVTI RSAFIEQAEN DSQLCVFAGA GIVEGSIPLL EWREIERKAM
     GLVSLLQQNQ L