MENF_ECOLI
ID MENF_ECOLI Reviewed; 431 AA.
AC P38051; P76479; P78297; Q47009; Q47704;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Isochorismate synthase MenF {ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000303|PubMed:8764478};
DE EC=5.4.4.2 {ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:17240978, ECO:0000269|PubMed:8764478, ECO:0000269|PubMed:9150206, ECO:0000269|PubMed:9795253};
DE AltName: Full=Isochorismate hydroxymutase {ECO:0000303|PubMed:8549818};
DE AltName: Full=Isochorismate mutase {ECO:0000255|HAMAP-Rule:MF_01935};
GN Name=menF {ECO:0000255|HAMAP-Rule:MF_01935}; Synonyms=yfbA;
GN OrderedLocusNames=b2265, JW2260;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8549818; DOI=10.1016/0014-5793(95)01436-5;
RA Mueller R., Dahm C., Schulte G., Leistner E.;
RT "An isochorismate hydroxymutase isogene in Escherichia coli.";
RL FEBS Lett. 378:131-134(1996).
RN [2]
RP SEQUENCE REVISION.
RA Mueller R.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / PL2024;
RX PubMed=8764478; DOI=10.1016/0378-1097(96)00173-5;
RA Daruwala R., Kwon O., Meganathan R., Hudspeth M.E.S.;
RT "A new isochorismate synthase specifically involved in menaquinone (vitamin
RT K2) biosynthesis encoded by the menF gene.";
RL FEMS Microbiol. Lett. 140:159-163(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-216.
RC STRAIN=K12;
RA Huisman G.W.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 216-431.
RX PubMed=2666397; DOI=10.1128/jb.171.8.4349-4354.1989;
RA Popp J.L.;
RT "Sequence and overexpression of the menD gene from Escherichia coli.";
RL J. Bacteriol. 171:4349-4354(1989).
RN [9]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP COFACTOR.
RX PubMed=9150206; DOI=10.1128/jb.179.10.3133-3138.1997;
RA Daruwala R., Bhattacharyya D.K., Kwon O., Meganathan R.;
RT "Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and
RT characterization of a new isochorismate synthase from Escherichia coli.";
RL J. Bacteriol. 179:3133-3138(1997).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=9795253; DOI=10.1016/s0304-4165(98)00089-0;
RA Dahm C., Muller R., Schulte G., Schmidt K., Leistner E.;
RT "The role of isochorismate hydroxymutase genes entC and menF in
RT enterobactin and menaquinone biosynthesis in Escherichia coli.";
RL Biochim. Biophys. Acta 1425:377-386(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-190; GLU-240;
RP LEU-255; ALA-344 AND ARG-387, AND ACTIVE SITES.
RX PubMed=17240978; DOI=10.1021/bi0608515;
RA Kolappan S., Zwahlen J., Zhou R., Truglio J.J., Tonge P.J., Kisker C.;
RT "Lysine 190 is the catalytic base in MenF, the menaquinone-specific
RT isochorismate synthase from Escherichia coli: implications for an enzyme
RT family.";
RL Biochemistry 46:946-953(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP COFACTOR.
RX PubMed=18453696; DOI=10.1107/s0907444908005477;
RA Parsons J.F., Shi K.M., Ladner J.E.;
RT "Structure of isochorismate synthase in complex with magnesium.";
RL Acta Crystallogr. D 64:607-610(2008).
CC -!- FUNCTION: Catalyzes the conversion of chorismate to isochorismate. Can
CC also catalyze the reverse reaction, but with a lower efficiency.
CC {ECO:0000269|PubMed:17240978, ECO:0000269|PubMed:8764478,
CC ECO:0000269|PubMed:9150206, ECO:0000269|PubMed:9795253}.
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 ECO:0000269|PubMed:17240978, ECO:0000269|PubMed:8764478,
CC ECO:0000269|PubMed:9150206, ECO:0000269|PubMed:9795253};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01935,
CC ECO:0000269|PubMed:17240978, ECO:0000269|PubMed:18453696,
CC ECO:0000269|PubMed:9150206, ECO:0000269|PubMed:9795253};
CC Note=Binds more tightly in the presence of chorismate.
CC {ECO:0000269|PubMed:17240978};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=119 uM for isochorismate (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9795253};
CC KM=166.9 uM for chorismate (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9795253};
CC KM=192 uM for chorismate {ECO:0000269|PubMed:17240978};
CC KM=195 uM for chorismate {ECO:0000269|PubMed:9150206};
CC KM=770 uM for magnesium {ECO:0000269|PubMed:17240978};
CC Vmax=91.7 pmol/sec/mg enzyme with chorismate as substrate (at pH 7.5
CC and 37 degrees Celsius) {ECO:0000269|PubMed:9795253};
CC Vmax=2.4 pmol/sec/mg enzyme with isochorismate as substrate (at pH
CC 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:9795253};
CC Note=kcat is 213 min(-1) for mutase activity with chorismate. kcat is
CC 176 min(-1) for mutase activity with chorismate in the presence of 30
CC mM of beta-mercaptoethanol (BME). kcat is 144.9 min(-1) for mutase
CC activity with chorismate (at pH 7.5 and 37 degrees Celsius). kcat is
CC 80 min(-1) for mutase activity with chorismate in the absence of 30
CC mM of beta-mercaptoethanol (BME). kcat is 3.8 min(-1) for mutase
CC activity with isochorismate (at pH 7.5 and 37 degrees Celsius.
CC {ECO:0000269|PubMed:17240978, ECO:0000269|PubMed:9150206,
CC ECO:0000269|PubMed:9795253};
CC pH dependence:
CC Optimum pH is between 7.5 and 8. The mutase activity decreases
CC sharply at pH 6.5 and 9 to about 20% of that observed at the optimum
CC pH. {ECO:0000269|PubMed:9150206, ECO:0000269|PubMed:9795253};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. At 60 degrees Celsius the
CC mutase activity is completely lost. {ECO:0000269|PubMed:9150206,
CC ECO:0000269|PubMed:9795253};
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, ECO:0000269|PubMed:8549818,
CC ECO:0000269|PubMed:9795253}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:9795253}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9150206}.
CC -!- DISRUPTION PHENOTYPE: Mutant produces only a trace of menaquinone.
CC {ECO:0000269|PubMed:9795253}.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M21787; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z50849; CAA90702.1; -; Genomic_DNA.
DR EMBL; U54790; AAC44303.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75325.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16092.1; -; Genomic_DNA.
DR EMBL; U58768; AAB02729.1; -; Genomic_DNA.
DR EMBL; M21787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G64997; G64997.
DR RefSeq; NP_416768.4; NC_000913.3.
DR RefSeq; WP_001191419.1; NZ_LN832404.1.
DR PDB; 2EUA; X-ray; 2.50 A; A/B=1-431.
DR PDB; 3BZM; X-ray; 1.95 A; A=1-431.
DR PDB; 3BZN; X-ray; 2.00 A; A=1-431.
DR PDBsum; 2EUA; -.
DR PDBsum; 3BZM; -.
DR PDBsum; 3BZN; -.
DR AlphaFoldDB; P38051; -.
DR SMR; P38051; -.
DR BioGRID; 4262080; 6.
DR DIP; DIP-10187N; -.
DR IntAct; P38051; 7.
DR STRING; 511145.b2265; -.
DR jPOST; P38051; -.
DR PaxDb; P38051; -.
DR PRIDE; P38051; -.
DR EnsemblBacteria; AAC75325; AAC75325; b2265.
DR EnsemblBacteria; BAA16092; BAA16092; BAA16092.
DR GeneID; 946712; -.
DR KEGG; ecj:JW2260; -.
DR KEGG; eco:b2265; -.
DR PATRIC; fig|1411691.4.peg.4471; -.
DR EchoBASE; EB2265; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_8_4_6; -.
DR InParanoid; P38051; -.
DR OMA; TGHGQSI; -.
DR PhylomeDB; P38051; -.
DR BioCyc; EcoCyc:MENF-MON; -.
DR BioCyc; MetaCyc:MENF-MON; -.
DR BRENDA; 5.4.4.2; 2026.
DR SABIO-RK; P38051; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00163.
DR EvolutionaryTrace; P38051; -.
DR PRO; PR:P38051; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008909; F:isochorismate synthase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Magnesium; Menaquinone biosynthesis;
KW Metal-binding; Reference proteome.
FT CHAIN 1..431
FT /note="Isochorismate synthase MenF"
FT /id="PRO_0000154147"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935,
FT ECO:0000269|PubMed:17240978"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935,
FT ECO:0000269|PubMed:17240978"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935,
FT ECO:0000269|PubMed:18453696"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01935,
FT ECO:0000269|PubMed:18453696"
FT MUTAGEN 190
FT /note="K->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:17240978"
FT MUTAGEN 240
FT /note="E->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:17240978"
FT MUTAGEN 255
FT /note="L->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:17240978"
FT MUTAGEN 344
FT /note="A->T: Lack of activity."
FT /evidence="ECO:0000269|PubMed:17240978"
FT MUTAGEN 387
FT /note="R->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:17240978"
FT CONFLICT 310..312
FT /note="VLR -> YC (in Ref. 3; AAC44303)"
FT /evidence="ECO:0000305"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 60..75
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2EUA"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 190..203
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 249..260
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 314..329
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:3BZM"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:3BZM"
FT TURN 366..369
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:3BZM"
FT STRAND 395..404
FT /evidence="ECO:0007829|PDB:3BZM"
FT HELIX 410..425
FT /evidence="ECO:0007829|PDB:3BZM"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3BZM"
SQ SEQUENCE 431 AA; 48765 MW; D081724F3329FE47 CRC64;
MQSLTTALEN LLRHLSQEIP ATPGIRVIDI PFPLKDAFDA LSWLASQQTY PQFYWQQRNG
DEEAVVLGAI TRFTSLDQAQ RFLRQHPEHA DLRIWGLNAF DPSQGNLLLP RLEWRRCGGK
ATLRLTLFSE SSLQHDAIQA KEFIATLVSI KPLPGLHLTT TREQHWPDKT GWTQLIELAT
KTIAEGELDK VVLARATDLH FASPVNAAAM MAASRRLNLN CYHFYMAFDG ENAFLGSSPE
RLWRRRDKAL RTEALAGTVA NNPDDKQAQQ LGEWLMADDK NQRENMLVVE DICQRLQADT
QTLDVLPPQV LRLRKVQHLR RCIWTSLNKA DDVICLHQLQ PTAAVAGLPR DLARQFIARH
EPFTREWYAG SAGYLSLQQS EFCVSLRSAK ISGNVVRLYA GAGIVRGSDP EQEWQEIDNK
AAGLRTLLQM E
