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UniProtKB - P38051 (MENF_ECOLI)

Entry version 169 (02 Dec 2020)
Sequence version 4 (01 Nov 1997)
Previous versions | rss
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
  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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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), Isochorismate synthase MenF (menF)
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD), 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH), 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
  4. o-succinylbenzoate synthase (menC), o-succinylbenzoate synthase (menC)
  5. 2-succinylbenzoate--CoA ligase (menE), 2-succinylbenzoate--CoA ligase (menE)
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB), 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI), 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei190Proton acceptorUniRule annotation1 Publication1
Active sitei240Proton donorUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi284MagnesiumUniRule annotation1 Publication1
Metal bindingi416MagnesiumUniRule annotation1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

  • menaquinone biosynthetic process Source: EcoCyc
Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase
Biological processMenaquinone biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:MENF-MONOMER
MetaCyc:MENF-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		5.4.4.2, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P38051

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00079
UPA01057;UER00163

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:menFUniRule annotation
Synonyms:yfbA
Ordered Locus Names:b2265, JW2260
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant produces only a trace of menaquinone.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001541471 – 431Isochorismate synthase MenFAdd BLAST431

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P38051

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P38051

PRoteomics IDEntifications database

More...PRIDEi		P38051

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262080, 6 interactors

Database of interacting proteins

More...DIPi		DIP-10187N

Protein interaction database and analysis system

More...IntActi		P38051, 7 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2265

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P38051

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P38051

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the isochorismate synthase family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1169, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006493_8_4_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P38051

Database for complete collections of gene phylogenies

More...PhylomeDBi		P38051

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.120.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01935, MenF, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005801, ADC_synthase
IPR015890, Chorismate_C
IPR004561, IsoChor_synthase
IPR034681, MenF

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00425, Chorismate_bind, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56322, SSF56322, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00543, isochor_syn, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD081724F3329FE47
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence M21787 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti310 – 312VLR → YC in AAC44303 (PubMed:8764478).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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.

Protein sequence database of the Protein Information Resource

More...PIRi		G64997

NCBI Reference Sequences

More...RefSeqi		NP_416768.4, NC_000913.3
WP_001191419.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75325; AAC75325; b2265
BAA16092; BAA16092; BAA16092

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946712

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2260
eco:b2265

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4471

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EUAX-ray2.50A/B1-431[»]
3BZMX-ray1.95A1-431[»]
3BZNX-ray2.00A1-431[»]
SMRiP38051
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262080, 6 interactors
DIPiDIP-10187N
IntActiP38051, 7 interactors
STRINGi511145.b2265

Proteomic databases

jPOSTiP38051
PaxDbiP38051
PRIDEiP38051

Genome annotation databases

EnsemblBacteriaiAAC75325; AAC75325; b2265
BAA16092; BAA16092; BAA16092
GeneIDi946712
KEGGiecj:JW2260
eco:b2265
PATRICifig|1411691.4.peg.4471

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB2265

Phylogenomic databases

eggNOGiCOG1169, Bacteria
HOGENOMiCLU_006493_8_4_6
InParanoidiP38051
PhylomeDBiP38051

Enzyme and pathway databases

UniPathwayiUPA00079
UPA01057;UER00163
BioCyciEcoCyc:MENF-MONOMER
MetaCyc:MENF-MONOMER
BRENDAi5.4.4.2, 2026
SABIO-RKiP38051

Miscellaneous databases

EvolutionaryTraceiP38051

Protein Ontology

More...PROi		PR:P38051

Family and domain databases

Gene3Di3.60.120.10, 1 hit
HAMAPiMF_01935, MenF, 1 hit
InterProiView protein in InterPro
IPR005801, ADC_synthase
IPR015890, Chorismate_C
IPR004561, IsoChor_synthase
IPR034681, MenF
PfamiView protein in Pfam
PF00425, Chorismate_bind, 1 hit
SUPFAMiSSF56322, SSF56322, 1 hit
TIGRFAMsiTIGR00543, isochor_syn, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMENF_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38051
Secondary accession number(s): P76479
, P78297, Q47009, Q47704
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: December 2, 2020
This is version 169 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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