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Protein

Isochorismate synthase MenF

Gene

menF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of chorismate to isochorismate. Can also catalyze the reverse reaction, but with a lower efficiency.4 Publications

Catalytic activityi

Chorismate = isochorismate.UniRule annotation4 Publications

Cofactori

Mg2+UniRule annotation4 PublicationsNote: Binds more tightly in the presence of chorismate.1 Publication

Kineticsi

kcat is 213 min(-1) for mutase activity with chorismate. kcat is 176 min(-1) for mutase activity with chorismate in the presence of 30 mM of beta-mercaptoethanol (BME). kcat is 144.9 min(-1) for mutase activity with chorismate (at pH 7.5 and 37 degrees Celsius). kcat is 80 min(-1) for mutase activity with chorismate in the absence of 30 mM of beta-mercaptoethanol (BME). kcat is 3.8 min(-1) for mutase activity with isochorismate (at pH 7.5 and 37 degrees Celsius.3 Publications

Manual assertion based on experiment ini

  1. KM=119 µM for isochorismate (at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=166.9 µM for chorismate (at pH 7.5 and 37 degrees Celsius)1 Publication
  3. KM=192 µM for chorismate1 Publication
  4. KM=195 µM for chorismate1 Publication
  5. KM=770 µM for magnesium1 Publication
  1. Vmax=91.7 pmol/sec/mg enzyme with chorismate as substrate (at pH 7.5 and 37 degrees Celsius)1 Publication
  2. Vmax=2.4 pmol/sec/mg enzyme with isochorismate as substrate (at pH 7.5 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 7.5 and 8. The mutase activity decreases sharply at pH 6.5 and 9 to about 20% of that observed at the optimum pH.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius. At 60 degrees Celsius the mutase activity is completely lost.2 Publications

Pathwayi: 1,4-dihydroxy-2-naphthoate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation2 Publications
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Isochorismate synthase MenF (menF)
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
  4. o-succinylbenzoate synthase (menC)
  5. 2-succinylbenzoate--CoA ligase (menE)
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI)
This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei190Proton acceptorUniRule annotation1 Publication1
Active sitei240Proton donorUniRule annotation1 Publication1
Metal bindingi284MagnesiumUniRule annotation1 Publication1
Metal bindingi416MagnesiumUniRule annotation1 Publication1

GO - Molecular functioni

  • isochorismate synthase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc

GO - Biological processi

  • menaquinone biosynthetic process Source: EcoCyc
  • salicylic acid biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:MENF-MONOMER.
ECOL316407:JW2260-MONOMER.
MetaCyc:MENF-MONOMER.
BRENDAi5.4.4.2. 2026.
SABIO-RKP38051.
UniPathwayiUPA00079.
UPA01057; UER00163.

Names & Taxonomyi

Protein namesi
Recommended name:
Isochorismate synthase MenF1 PublicationUniRule annotation (EC:5.4.4.2UniRule annotation4 Publications)
Alternative name(s):
Isochorismate hydroxymutase1 Publication
Isochorismate mutaseUniRule annotation
Gene namesi
Name:menFUniRule annotation
Synonyms:yfbA
Ordered Locus Names:b2265, JW2260
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12362. menF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutant produces only a trace of menaquinone.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi190K → A: Lack of activity. 1 Publication1
Mutagenesisi240E → Q: Lack of activity. 1 Publication1
Mutagenesisi255L → A: Decrease in activity. 1 Publication1
Mutagenesisi344A → T: Lack of activity. 1 Publication1
Mutagenesisi387R → A: Lack of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001541471 – 431Isochorismate synthase MenFAdd BLAST431

Proteomic databases

PaxDbiP38051.
PRIDEiP38051.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262080. 6 interactors.
DIPiDIP-10187N.
IntActiP38051. 7 interactors.
MINTiMINT-1275996.
STRINGi511145.b2265.

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 15Combined sources14
Beta strandi21 – 32Combined sources12
Helixi40 – 45Combined sources6
Beta strandi52 – 56Combined sources5
Beta strandi60 – 75Combined sources16
Helixi76 – 84Combined sources9
Helixi87 – 89Combined sources3
Beta strandi94 – 98Combined sources5
Beta strandi105 – 117Combined sources13
Beta strandi120 – 131Combined sources12
Helixi133 – 146Combined sources14
Beta strandi160 – 167Combined sources8
Helixi169 – 185Combined sources17
Beta strandi190 – 203Combined sources14
Helixi207 – 217Combined sources11
Beta strandi221 – 227Combined sources7
Beta strandi229 – 238Combined sources10
Beta strandi241 – 246Combined sources6
Beta strandi249 – 260Combined sources12
Helixi265 – 275Combined sources11
Helixi281 – 296Combined sources16
Helixi297 – 299Combined sources3
Beta strandi309 – 312Combined sources4
Beta strandi314 – 329Combined sources16
Helixi332 – 339Combined sources8
Turni343 – 345Combined sources3
Beta strandi346 – 349Combined sources4
Helixi350 – 360Combined sources11
Turni366 – 369Combined sources4
Beta strandi370 – 375Combined sources6
Beta strandi377 – 384Combined sources8
Beta strandi387 – 392Combined sources6
Beta strandi395 – 404Combined sources10
Helixi410 – 425Combined sources16
Turni426 – 428Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EUAX-ray2.50A/B1-431[»]
3BZMX-ray1.95A1-431[»]
3BZNX-ray2.00A1-431[»]
ProteinModelPortaliP38051.
SMRiP38051.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38051.

Family & Domainsi

Sequence similaritiesi

Belongs to the isochorismate synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105E4F. Bacteria.
COG1169. LUCA.
HOGENOMiHOG000028186.
InParanoidiP38051.
KOiK02552.
OMAiRCIWTEL.
PhylomeDBiP38051.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
HAMAPiMF_01935. MenF. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR015890. Chorismate_C.
IPR004561. IsoChor_synthase.
[Graphical view]
PfamiPF00425. Chorismate_bind. 1 hit.
[Graphical view]
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00543. isochor_syn. 1 hit.

Sequencei

Sequence statusi: Complete.

P38051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSLTTALEN LLRHLSQEIP ATPGIRVIDI PFPLKDAFDA LSWLASQQTY
60 70 80 90 100
PQFYWQQRNG DEEAVVLGAI TRFTSLDQAQ RFLRQHPEHA DLRIWGLNAF
110 120 130 140 150
DPSQGNLLLP RLEWRRCGGK ATLRLTLFSE SSLQHDAIQA KEFIATLVSI
160 170 180 190 200
KPLPGLHLTT TREQHWPDKT GWTQLIELAT KTIAEGELDK VVLARATDLH
210 220 230 240 250
FASPVNAAAM MAASRRLNLN CYHFYMAFDG ENAFLGSSPE RLWRRRDKAL
260 270 280 290 300
RTEALAGTVA NNPDDKQAQQ LGEWLMADDK NQRENMLVVE DICQRLQADT
310 320 330 340 350
QTLDVLPPQV LRLRKVQHLR RCIWTSLNKA DDVICLHQLQ PTAAVAGLPR
360 370 380 390 400
DLARQFIARH EPFTREWYAG SAGYLSLQQS EFCVSLRSAK ISGNVVRLYA
410 420 430
GAGIVRGSDP EQEWQEIDNK AAGLRTLLQM E
Length:431
Mass (Da):48,765
Last modified:November 1, 1997 - v4
Checksum:iD081724F3329FE47
GO

Sequence cautioni

The sequence M21787 differs from that shown. Reason: Frameshift at positions 270, 310 and 341.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti310 – 312VLR → YC in AAC44303 (PubMed:8764478).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50849 Genomic DNA. Translation: CAA90702.1.
U54790 Genomic DNA. Translation: AAC44303.1.
U00096 Genomic DNA. Translation: AAC75325.2.
AP009048 Genomic DNA. Translation: BAA16092.1.
U58768 Genomic DNA. Translation: AAB02729.1.
M21787 Genomic DNA. No translation available.
PIRiG64997.
RefSeqiNP_416768.4. NC_000913.3.
WP_001191419.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75325; AAC75325; b2265.
BAA16092; BAA16092; BAA16092.
GeneIDi946712.
KEGGiecj:JW2260.
eco:b2265.
PATRICi32119897. VBIEscCol129921_2358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50849 Genomic DNA. Translation: CAA90702.1.
U54790 Genomic DNA. Translation: AAC44303.1.
U00096 Genomic DNA. Translation: AAC75325.2.
AP009048 Genomic DNA. Translation: BAA16092.1.
U58768 Genomic DNA. Translation: AAB02729.1.
M21787 Genomic DNA. No translation available.
PIRiG64997.
RefSeqiNP_416768.4. NC_000913.3.
WP_001191419.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EUAX-ray2.50A/B1-431[»]
3BZMX-ray1.95A1-431[»]
3BZNX-ray2.00A1-431[»]
ProteinModelPortaliP38051.
SMRiP38051.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262080. 6 interactors.
DIPiDIP-10187N.
IntActiP38051. 7 interactors.
MINTiMINT-1275996.
STRINGi511145.b2265.

Proteomic databases

PaxDbiP38051.
PRIDEiP38051.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75325; AAC75325; b2265.
BAA16092; BAA16092; BAA16092.
GeneIDi946712.
KEGGiecj:JW2260.
eco:b2265.
PATRICi32119897. VBIEscCol129921_2358.

Organism-specific databases

EchoBASEiEB2265.
EcoGeneiEG12362. menF.

Phylogenomic databases

eggNOGiENOG4105E4F. Bacteria.
COG1169. LUCA.
HOGENOMiHOG000028186.
InParanoidiP38051.
KOiK02552.
OMAiRCIWTEL.
PhylomeDBiP38051.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00163.
BioCyciEcoCyc:MENF-MONOMER.
ECOL316407:JW2260-MONOMER.
MetaCyc:MENF-MONOMER.
BRENDAi5.4.4.2. 2026.
SABIO-RKP38051.

Miscellaneous databases

EvolutionaryTraceiP38051.
PROiP38051.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
HAMAPiMF_01935. MenF. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR015890. Chorismate_C.
IPR004561. IsoChor_synthase.
[Graphical view]
PfamiPF00425. Chorismate_bind. 1 hit.
[Graphical view]
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00543. isochor_syn. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMENF_ECOLI
AccessioniPrimary (citable) accession number: P38051
Secondary accession number(s): P76479
, P78297, Q47009, Q47704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.