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Protein

Anthranilate synthase component 1

Gene

trpE

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 4 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+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

Cooperatively feedback inhibited by tryptophan.1 Publication

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. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
  4. Indole-3-glycerol phosphate synthase (trpC)
  5. Tryptophan synthase beta chain 2 (trpB2), Tryptophan synthase beta chain 1 (trpB1), 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 sitei31TryptophanBy similarity1
Metal bindingi269MagnesiumBy similarity1
Binding sitei357ChorismateBy similarity1
Binding sitei377ChorismateBy similarity1
Binding sitei393Chorismate; via amide nitrogenBy similarity1
Metal bindingi406MagnesiumBy 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

BioCyciMetaCyc:MONOMER-3603.
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:SSO0893
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001541321 – 421Anthranilate synthase component 1Add BLAST421

Interactioni

Subunit structurei

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).1 Publication

Protein-protein interaction databases

DIPiDIP-6202N.
IntActiQ06128. 1 interactor.
MINTiMINT-102245.
STRINGi273057.SSO0893.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 5Combined sources5
Helixi6 – 8Combined sources3
Helixi12 – 22Combined sources11
Beta strandi24 – 30Combined sources7
Beta strandi41 – 46Combined sources6
Beta strandi52 – 54Combined sources3
Helixi58 – 63Combined sources6
Turni64 – 68Combined sources5
Beta strandi75 – 77Combined sources3
Beta strandi79 – 86Combined sources8
Helixi88 – 93Combined sources6
Beta strandi103 – 105Combined sources3
Beta strandi109 – 113Combined sources5
Beta strandi116 – 122Combined sources7
Helixi123 – 125Combined sources3
Beta strandi127 – 132Combined sources6
Beta strandi146 – 155Combined sources10
Helixi157 – 173Combined sources17
Beta strandi177 – 191Combined sources15
Helixi194 – 203Combined sources10
Beta strandi207 – 214Combined sources8
Beta strandi217 – 224Combined sources8
Beta strandi226 – 231Combined sources6
Beta strandi234 – 237Combined sources4
Beta strandi240 – 245Combined sources6
Helixi250 – 261Combined sources12
Helixi264 – 282Combined sources19
Beta strandi291 – 300Combined sources10
Beta strandi302 – 315Combined sources14
Helixi321 – 328Combined sources8
Helixi332 – 334Combined sources3
Beta strandi335 – 338Combined sources4
Helixi339 – 349Combined sources11
Beta strandi350 – 353Combined sources4
Turni355 – 358Combined sources4
Beta strandi359 – 365Combined sources7
Beta strandi370 – 375Combined sources6
Beta strandi377 – 382Combined sources6
Beta strandi385 – 394Combined sources10
Helixi400 – 417Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QDLX-ray2.50A1-421[»]
ProteinModelPortaliQ06128.
SMRiQ06128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06128.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni207 – 209Tryptophan bindingBy similarity3
Regioni242 – 243Chorismate bindingBy similarity2
Regioni391 – 393Chorismate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG02014. Archaea.
COG0147. LUCA.
HOGENOMiHOG000025142.
InParanoidiQ06128.
KOiK01657.
OMAiRIFQCEV.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR010116. Anthranilate_synth_I_arc_typ.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR01820. TrpE-arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q06128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVHPISEFA SPFEVFKCIE RDFKVAGLLE SIGGPQYKAR YSVIAWSTNG
60 70 80 90 100
YLKIHDDPVN ILNGYLKDLK LADIPGLFKG GMIGYISYDA VRFWEKIRDL
110 120 130 140 150
KPAAEDWPYA EFFTPDNIII YDHNEGKVYV NADLSSVGGC GDIGEFKVSF
160 170 180 190 200
YDESLNKNSY ERIVSESLEY IRSGYIFQVV LSRFYRYIFS GDPLRIYYNL
210 220 230 240 250
RRINPSPYMF YLKFDEKYLI GSSPELLFRV QDNIVETYPI AGTRPRGADQ
260 270 280 290 300
EEDLKLELEL MNSEKDKAEH LMLVDLARND LGKVCVPGTV KVPELMYVEK
310 320 330 340 350
YSHVQHIVSK VIGTLKKKYN ALNVLSATFP AGTVSGAPKP MAMNIIETLE
360 370 380 390 400
EYKRGPYAGA VGFISADGNA EFAIAIRTAF LNKELLRIHA GAGIVYDSNP
410 420
ESEYFETEHK LKALKTAIGV R
Length:421
Mass (Da):47,652
Last modified:June 20, 2001 - v2
Checksum:iBD49BD7771ECC6EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti337A → R in AAA73379 (PubMed:8416906).Curated1
Sequence conflicti337A → R in CAA90311 (PubMed:9016772).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98048 Genomic DNA. Translation: AAA73379.1.
Z50014 Genomic DNA. Translation: CAA90311.1.
AE006641 Genomic DNA. Translation: AAK41175.1.
PIRiH90239.
JC5323.
RefSeqiWP_009992309.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK41175; AAK41175; SSO0893.
GeneIDi27427213.
KEGGisso:SSO0893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98048 Genomic DNA. Translation: AAA73379.1.
Z50014 Genomic DNA. Translation: CAA90311.1.
AE006641 Genomic DNA. Translation: AAK41175.1.
PIRiH90239.
JC5323.
RefSeqiWP_009992309.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QDLX-ray2.50A1-421[»]
ProteinModelPortaliQ06128.
SMRiQ06128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6202N.
IntActiQ06128. 1 interactor.
MINTiMINT-102245.
STRINGi273057.SSO0893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK41175; AAK41175; SSO0893.
GeneIDi27427213.
KEGGisso:SSO0893.

Phylogenomic databases

eggNOGiarCOG02014. Archaea.
COG0147. LUCA.
HOGENOMiHOG000025142.
InParanoidiQ06128.
KOiK01657.
OMAiRIFQCEV.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
BioCyciMetaCyc:MONOMER-3603.

Miscellaneous databases

EvolutionaryTraceiQ06128.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR010116. Anthranilate_synth_I_arc_typ.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR01820. TrpE-arch. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTRPE_SULSO
AccessioniPrimary (citable) accession number: Q06128
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 20, 2001
Last modified: November 2, 2016
This is version 133 of the entry and version 2 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, 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.