ID   MENF_HAEIN              Reviewed;         430 AA.
AC   P44613;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=HI_0285;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21947.1; -; Genomic_DNA.
DR   PIR; E64059; E64059.
DR   RefSeq; NP_438452.1; NC_000907.1.
DR   AlphaFoldDB; P44613; -.
DR   SMR; P44613; -.
DR   STRING; 71421.HI_0285; -.
DR   EnsemblBacteria; AAC21947; AAC21947; HI_0285.
DR   KEGG; hin:HI_0285; -.
DR   PATRIC; fig|71421.8.peg.300; -.
DR   eggNOG; COG1169; Bacteria.
DR   HOGENOM; CLU_006493_8_4_6; -.
DR   OMA; TGHGQSI; -.
DR   PhylomeDB; P44613; -.
DR   BioCyc; HINF71421:G1GJ1-303-MON; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00163.
DR   Proteomes; UP000000579; 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   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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   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..430
FT                   /note="Isochorismate synthase MenF"
FT                   /id="PRO_0000154148"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01935"
FT   BINDING         281
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   430 AA;  48466 MW;  3BA131F8B62A1B38 CRC64;
     MYLKQNLMSY LAQAIGELKS QIHAYLQQST NELVRFQVKL DKVDLLAWLK GQSAYPQFYL
     HFRDEEKALA ALGAVQSFSQ LNLAQEFIEE SGFPLVGGLQ FQGTAQFVLP KMLVEQDNKG
     TLVSFFVKNE QSANDTLAHL KTFENLTALS ALPKQIPLHT ELRANERTWC DWVNQALVEI
     KSGELTKIVL ANETTFHLKQ AINAYDFLAE SEKQNQGCYH FLWAENSHSV FVGSTPERLF
     AREYNLLLTE ALAGTASVSE SEEETQSQAN WLLNDEKNLK ENWLVVEDIS QNLRKQVESF
     DVSNVELKPL RKVQHLIRKI RANLTAHYAD VNILKAIHPT AAVSGLPQQQ AKMILSEIET
     FDRGWYAGTL GVMSDVCSEF CVAIRSAFIE GHRIRVFAGA GIVAGSQPLE EWKEIERKAA
     GLISLFAEEK