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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

Manual assertion based on experiment ini

  • Ref.7
    "Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhimurium. Evidence for an amino-terminal regulatory site."
    Caligiuri M.G., Bauerle R.
    J. Biol. Chem. 266:8328-8335(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-39; SER-40; ALA-41; ARG-128; CYS-174; ASN-288; PRO-289; MET-293; PHE-294; GLY-305; ARG-402; GLY-460; CYS-465 AND HIS-515.

  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)DescriptionActionsGraphical viewLength
Binding sitei40Tryptophan1 Publication1
Binding sitei50Tryptophan1 Publication1
Metal bindingi361MagnesiumBy similarity1
Binding sitei449ChorismateBy similarity1
Binding sitei469ChorismateBy similarity1
Binding sitei485Chorismate; via amide nitrogenBy similarity1
Metal bindingi498MagnesiumBy similarity1

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

ChEMBLiCHEMBL1075109.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001541101 – 520Anthranilate synthase component 1Add BLAST520

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 interactor.
MINTiMINT-189120.
STRINGi99287.STM1723.

Chemistry databases

BindingDBiP00898.

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 15Combined sources7
Helixi21 – 29Combined sources9
Beta strandi33 – 39Combined sources7
Helixi43 – 45Combined sources3
Beta strandi50 – 64Combined sources15
Beta strandi67 – 74Combined sources8
Helixi75 – 78Combined sources4
Helixi80 – 85Combined sources6
Beta strandi93 – 97Combined sources5
Beta strandi100 – 104Combined sources5
Helixi114 – 118Combined sources5
Helixi125 – 132Combined sources8
Beta strandi143 – 150Combined sources8
Helixi152 – 157Combined sources6
Beta strandi167 – 169Combined sources3
Beta strandi172 – 185Combined sources14
Turni186 – 189Combined sources4
Beta strandi190 – 197Combined sources8
Helixi202 – 220Combined sources19
Beta strandi237 – 240Combined sources4
Helixi242 – 257Combined sources16
Beta strandi262 – 264Combined sources3
Beta strandi267 – 273Combined sources7
Helixi277 – 287Combined sources11
Beta strandi291 – 297Combined sources7
Beta strandi302 – 309Combined sources8
Beta strandi311 – 315Combined sources5
Turni316 – 319Combined sources4
Beta strandi320 – 323Combined sources4
Beta strandi326 – 331Combined sources6
Helixi342 – 354Combined sources13
Helixi356 – 376Combined sources21
Beta strandi383 – 392Combined sources10
Beta strandi394 – 407Combined sources14
Helixi413 – 420Combined sources8
Helixi424 – 426Combined sources3
Beta strandi427 – 430Combined sources4
Helixi431 – 442Combined sources12
Turni447 – 450Combined sources4
Beta strandi451 – 457Combined sources7
Beta strandi462 – 466Combined sources5
Beta strandi469 – 474Combined sources6
Beta strandi477 – 483Combined sources7
Helixi492 – 513Combined sources22

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00898.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni291 – 293Tryptophan binding3
Regioni328 – 329Chorismate bindingBy similarity2
Regioni483 – 485Chorismate bindingBy similarity3

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)DescriptionActionsGraphical viewLength
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:
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90A1-520[»]
ProteinModelPortaliP00898.
SMRiP00898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00898. 1 interactor.
MINTiMINT-189120.
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.
PATRICi32381959. VBISalEnt20916_1819.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.

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: November 2, 2016
This is version 139 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.