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Protein

Anthranilate synthase component 1

Gene

trpE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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

Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Cooperatively feedback inhibited by tryptophan.3 Publications

<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 12 (sec-1) for chorismate.1 Publication
  1. KM=2.3 µM for chorismate1 Publication
  2. KM=4 µM for anthranilate (with the dimeric form and for the phosphoribosyltransferase activity at pH 7.5)2 Publications
  3. KM=6 µM for anthranilate (with the monomeric form and for the phosphoribosyltransferase activity at pH 7.5)2 Publications
  4. KM=10 µM for phosphoribosylpyrophosphate (with the monomeric and dimeric forms and for the phosphoribosyltransferase activity at pH 7.5)2 Publications
  5. KM=30 µM for magnesium ion (with the monomeric and dimeric forms and for the phosphoribosyltransferase activity at pH 7.5)2 Publications
  1. Vmax=5800 nmol/min/mg enzyme (with the dimeric form and for the phosphoribosyltransferase activity at pH 7.5)2 Publications
  2. Vmax=4700 nmol/min/mg enzyme (for the monomeric form at pH 7.5)2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional protein TrpGD (trpGD), Anthranilate synthase component 1 (trpE)
  2. Bifunctional protein TrpGD (trpGD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei40Tryptophan1 Publication1
Binding sitei50Tryptophan1 Publication1
<p>This subsection of the ‘Function’ 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 bindingi361MagnesiumBy similarity1
Binding sitei449ChorismateBy similarity1
Binding sitei469ChorismateBy similarity1
Binding sitei485Chorismate; via amide nitrogenBy similarity1
Metal bindingi498MagnesiumBy similarity1

<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

GO - Biological processi

<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 functionAllosteric enzyme, Lyase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SENT99287:STM1723-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00898

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

More...
UniPathwayi
UPA00035;UER00040

<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_and_taxonomy_section">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:
Anthranilate synthase component 1 (EC:4.1.3.27)
Short name:
AS
Short name:
ASI
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:trpE
Ordered Locus Names:STM1723
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri99287 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001014 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi39E → K: Complete loss of feedback control by tryptophan. 1 Publication1
Mutagenesisi40S → F: Complete loss of feedback control by tryptophan. 1 Publication1
Mutagenesisi41A → V: Decrease in feedback control by tryptophan. 1 Publication1
Mutagenesisi128R → H: Almost no change in feedback control by tryptophan. 1 Publication1
Mutagenesisi174C → Y: Almost no change in feedback control by tryptophan. 1 Publication1
Mutagenesisi288N → D: Decrease in feedback control by tryptophan. 1 Publication1
Mutagenesisi289P → L: Decrease in feedback control by tryptophan. 1 Publication1
Mutagenesisi293M → T: Complete loss of feedback control by tryptophan. 1 Publication1
Mutagenesisi294F → L: Decrease in feedback control by tryptophan. 1 Publication1
Mutagenesisi305G → S: Decrease in feedback control by tryptophan. 1 Publication1
Mutagenesisi402R → W: Almost no change in feedback control by tryptophan. 1 Publication1
Mutagenesisi460G → D: Almost no change in feedback control by tryptophan. 1 Publication1
Mutagenesisi465C → Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate. 1 Publication1
Mutagenesisi515H → Y: Almost no change in feedback control by tryptophan. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075109

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001541101 – 520Anthranilate synthase component 1Add BLAST520

Proteomic databases

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

More...
PaxDbi
P00898

PRoteomics IDEntifications database

More...
PRIDEi
P00898

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. In fact, exists in a monomer-dimer equilibrium in solution, shifted spontaneously in favor of the dimer; the monomer has a reduced activity compared with the dimer. Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE) (Potential).Curated

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P00898, 1 interactor

Molecular INTeraction database

More...
MINTi
P00898

STRING: functional protein association networks

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STRINGi
99287.STM1723

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00898

<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

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00898

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

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SMRi
P00898

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00898

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni291 – 293Tryptophan binding3
Regioni328 – 329Chorismate bindingBy similarity2
Regioni483 – 485Chorismate bindingBy similarity3

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CRQ Bacteria
COG0147 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000025144

KEGG Orthology (KO)

More...
KOi
K01657

Identification of Orthologs from Complete Genome Data

More...
OMAi
AYRSFMN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00898

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005801 ADC_synthase
IPR019999 Anth_synth_I-like
IPR006805 Anth_synth_I_N
IPR005257 Anth_synth_I_TrpE
IPR015890 Chorismate_C

The PANTHER Classification System

More...
PANTHERi
PTHR11236:SF22 PTHR11236:SF22, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04715 Anth_synt_I_N, 1 hit
PF00425 Chorismate_bind, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001373 TrpE, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00095 ANTSNTHASEI

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56322 SSF56322, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00565 trpE_proteo, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P00898-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQTPKPTLEL LTCDAAYREN PTALFHQVCG DRPATLLLES ADIDSKDDLK
60 70 80 90 100
SLLLVDSALR ITALGDTVTI QALSDNGASL LPLLDTALPA GVENDVLPAG
110 120 130 140 150
RVLRFPPVSP LLDEDARLCS LSVFDAFRLL QGVVNIPTQE REAMFFGGLF
160 170 180 190 200
AYDLVAGFEA LPHLEAGNNC PDYCFYLAET LMVIDHQKKS TRIQASLFTA
210 220 230 240 250
SDREKQRLNA RLAYLSQQLT QPAPPLPVTP VPDMRCECNQ SDDAFGAVVR
260 270 280 290 300
QLQKAIRAGE IFQVVPSRRF SLPCPSPLAA YYVLKKSNPS PYMFFMQDND
310 320 330 340 350
FTLFGASPES SLKYDAASRQ IEIYPIAGTR PRGRRADGTL DRDLDSRIEL
360 370 380 390 400
DMRTDHKELS EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV
410 420 430 440 450
SRVVGELRHD LDALHAYRAC MNMGTLSGAP KVRAMQLIAD AEGQRRGSYG
460 470 480 490 500
GAVGYFTAHG DLDTCIVIRS ALVENGIATV QAGAGIVLDS VPQSEADETR
510 520
NKARAVLRAI ATAHHAQETF
Length:520
Mass (Da):57,088
Last modified:January 23, 2002 - v3
<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:iB120E903DB7F8329
GO

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 conflicti61I → F in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti70I → S in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti164L → H in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti179E → G in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti187Q → R in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti348I → T in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti359 – 360LS → PC in CAA24668 (PubMed:7042989).Curated2
Sequence conflicti368L → P in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti395Y → C in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti397M → I in CAA24668 (PubMed:7042989).Curated1
Sequence conflicti481Q → R in CAA24668 (PubMed:7042989).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
V01378 Genomic DNA Translation: CAA24668.1
AE006468 Genomic DNA Translation: AAL20641.1
M24960 Genomic DNA Translation: AAA27238.1
J01811 Genomic DNA Translation: AAA57311.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A92878 NNEB1T

NCBI Reference Sequences

More...
RefSeqi
NP_460682.1, NC_003197.2
WP_001194371.1, NC_003197.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAL20641; AAL20641; STM1723

Database of genes from NCBI RefSeq genomes

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GeneIDi
1253242

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
stm:STM1723

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|99287.12.peg.1819

<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
V01378 Genomic DNA Translation: CAA24668.1
AE006468 Genomic DNA Translation: AAL20641.1
M24960 Genomic DNA Translation: AAA27238.1
J01811 Genomic DNA Translation: AAA57311.1
PIRiA92878 NNEB1T
RefSeqiNP_460682.1, NC_003197.2
WP_001194371.1, NC_003197.2

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
1I1QX-ray1.90A1-520[»]
ProteinModelPortaliP00898
SMRiP00898
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00898, 1 interactor
MINTiP00898
STRINGi99287.STM1723

Chemistry databases

BindingDBiP00898
ChEMBLiCHEMBL1075109

Proteomic databases

PaxDbiP00898
PRIDEiP00898

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20641; AAL20641; STM1723
GeneIDi1253242
KEGGistm:STM1723
PATRICifig|99287.12.peg.1819

Phylogenomic databases

eggNOGiENOG4105CRQ Bacteria
COG0147 LUCA
HOGENOMiHOG000025144
KOiK01657
OMAiAYRSFMN
PhylomeDBiP00898

Enzyme and pathway databases

UniPathwayi
UPA00035;UER00040

BioCyciSENT99287:STM1723-MONOMER
SABIO-RKiP00898

Miscellaneous databases

EvolutionaryTraceiP00898

Family and domain databases

Gene3Di3.60.120.10, 1 hit
InterProiView protein in InterPro
IPR005801 ADC_synthase
IPR019999 Anth_synth_I-like
IPR006805 Anth_synth_I_N
IPR005257 Anth_synth_I_TrpE
IPR015890 Chorismate_C
PANTHERiPTHR11236:SF22 PTHR11236:SF22, 1 hit
PfamiView protein in Pfam
PF04715 Anth_synt_I_N, 1 hit
PF00425 Chorismate_bind, 1 hit
PIRSFiPIRSF001373 TrpE, 1 hit
PRINTSiPR00095 ANTSNTHASEI
SUPFAMiSSF56322 SSF56322, 1 hit
TIGRFAMsiTIGR00565 trpE_proteo, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiTRPE_SALTY
<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: P00898
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2002
Last modified: December 5, 2018
This is version 150 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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