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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-Experimental evidence at protein leveli

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

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Enzyme regulationi

Cooperatively feedback inhibited by tryptophan.3 Publications

Kineticsi

Kcat is 12 (sec-1) for chorismate.1 Publication

  1. KM=2.3 µM for chorismate (PubMed:2022650)2 Publications
  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

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 beta chain (trpB), Tryptophan synthase alpha chain (trpA)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401Tryptophan1 Publication
Binding sitei50 – 501Tryptophan1 Publication
Metal bindingi361 – 3611MagnesiumBy similarity
Binding sitei449 – 4491ChorismateBy similarity
Binding sitei469 – 4691ChorismateBy similarity
Binding sitei485 – 4851Chorismate; via amide nitrogenBy similarity
Metal bindingi498 – 4981MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1732-MONOMER.
UniPathwayiUPA00035; UER00040.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate synthase component 1 (EC:4.1.3.27)
Short name:
AS
Short name:
ASI
Gene namesi
Name:trpE
Ordered Locus Names:STM1723
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391E → K: Complete loss of feedback control by tryptophan. 1 Publication
Mutagenesisi40 – 401S → F: Complete loss of feedback control by tryptophan. 1 Publication
Mutagenesisi41 – 411A → V: Decrease in feedback control by tryptophan. 1 Publication
Mutagenesisi128 – 1281R → H: Almost no change in feedback control by tryptophan. 1 Publication
Mutagenesisi174 – 1741C → Y: Almost no change in feedback control by tryptophan. 1 Publication
Mutagenesisi288 – 2881N → D: Decrease in feedback control by tryptophan. 1 Publication
Mutagenesisi289 – 2891P → L: Decrease in feedback control by tryptophan. 1 Publication
Mutagenesisi293 – 2931M → T: Complete loss of feedback control by tryptophan. 1 Publication
Mutagenesisi294 – 2941F → L: Decrease in feedback control by tryptophan. 1 Publication
Mutagenesisi305 – 3051G → S: Decrease in feedback control by tryptophan. 1 Publication
Mutagenesisi402 – 4021R → W: Almost no change in feedback control by tryptophan. 1 Publication
Mutagenesisi460 – 4601G → D: Almost no change in feedback control by tryptophan. 1 Publication
Mutagenesisi465 – 4651C → Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate. 1 Publication
Mutagenesisi515 – 5151H → Y: Almost no change in feedback control by tryptophan. 1 Publication

Chemistry

ChEMBLiCHEMBL1075109.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Anthranilate synthase component 1PRO_0000154110Add
BLAST

Proteomic databases

PaxDbiP00898.
PRIDEiP00898.

Interactioni

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

IntActiP00898. 1 interaction.
MINTiMINT-189120.
STRINGi99287.STM1723.

Chemistry

BindingDBiP00898.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 157Combined sources
Helixi21 – 299Combined sources
Beta strandi33 – 397Combined sources
Helixi43 – 453Combined sources
Beta strandi50 – 6415Combined sources
Beta strandi67 – 748Combined sources
Helixi75 – 784Combined sources
Helixi80 – 856Combined sources
Beta strandi93 – 975Combined sources
Beta strandi100 – 1045Combined sources
Helixi114 – 1185Combined sources
Helixi125 – 1328Combined sources
Beta strandi143 – 1508Combined sources
Helixi152 – 1576Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi172 – 18514Combined sources
Turni186 – 1894Combined sources
Beta strandi190 – 1978Combined sources
Helixi202 – 22019Combined sources
Beta strandi237 – 2404Combined sources
Helixi242 – 25716Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi267 – 2737Combined sources
Helixi277 – 28711Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi302 – 3098Combined sources
Beta strandi311 – 3155Combined sources
Turni316 – 3194Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi326 – 3316Combined sources
Helixi342 – 35413Combined sources
Helixi356 – 37621Combined sources
Beta strandi383 – 39210Combined sources
Beta strandi394 – 40714Combined sources
Helixi413 – 4208Combined sources
Helixi424 – 4263Combined sources
Beta strandi427 – 4304Combined sources
Helixi431 – 44212Combined sources
Turni447 – 4504Combined sources
Beta strandi451 – 4577Combined sources
Beta strandi462 – 4665Combined sources
Beta strandi469 – 4746Combined sources
Beta strandi477 – 4837Combined sources
Helixi492 – 51322Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90A1-520[»]
ProteinModelPortaliP00898.
SMRiP00898. Positions 5-516.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00898.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 2933Tryptophan binding
Regioni328 – 3292Chorismate bindingBy similarity
Regioni483 – 4853Chorismate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CRQ. Bacteria.
COG0147. LUCA.
HOGENOMiHOG000025144.
KOiK01657.
OMAiMQDQDFT.
PhylomeDBiP00898.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR005257. Anth_synth_I_TrpE.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF001373. TrpE. 1 hit.
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00565. trpE_proteo. 1 hit.

Sequencei

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
Checksum:iB120E903DB7F8329
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611I → F in CAA24668 (PubMed:7042989).Curated
Sequence conflicti70 – 701I → S in CAA24668 (PubMed:7042989).Curated
Sequence conflicti164 – 1641L → H in CAA24668 (PubMed:7042989).Curated
Sequence conflicti179 – 1791E → G in CAA24668 (PubMed:7042989).Curated
Sequence conflicti187 – 1871Q → R in CAA24668 (PubMed:7042989).Curated
Sequence conflicti348 – 3481I → T in CAA24668 (PubMed:7042989).Curated
Sequence conflicti359 – 3602LS → PC in CAA24668 (PubMed:7042989).Curated
Sequence conflicti368 – 3681L → P in CAA24668 (PubMed:7042989).Curated
Sequence conflicti395 – 3951Y → C in CAA24668 (PubMed:7042989).Curated
Sequence conflicti397 – 3971M → I in CAA24668 (PubMed:7042989).Curated
Sequence conflicti481 – 4811Q → R in CAA24668 (PubMed:7042989).Curated

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_003197.1.
WP_001194371.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20641; AAL20641; STM1723.
GeneIDi1253242.
KEGGistm:STM1723.
PATRICi32381959. VBISalEnt20916_1819.

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_003197.1.
WP_001194371.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90A1-520[»]
ProteinModelPortaliP00898.
SMRiP00898. Positions 5-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00898. 1 interaction.
MINTiMINT-189120.
STRINGi99287.STM1723.

Chemistry

BindingDBiP00898.
ChEMBLiCHEMBL1075109.

Proteomic databases

PaxDbiP00898.
PRIDEiP00898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20641; AAL20641; STM1723.
GeneIDi1253242.
KEGGistm:STM1723.
PATRICi32381959. VBISalEnt20916_1819.

Phylogenomic databases

eggNOGiENOG4105CRQ. Bacteria.
COG0147. LUCA.
HOGENOMiHOG000025144.
KOiK01657.
OMAiMQDQDFT.
PhylomeDBiP00898.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
BioCyciSENT99287:GCTI-1732-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00898.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR005257. Anth_synth_I_TrpE.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF001373. TrpE. 1 hit.
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00565. trpE_proteo. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTRPE_SALTY
AccessioniPrimary (citable) accession number: P00898
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2002
Last modified: September 7, 2016
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, 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

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.