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Q06128 (TRPE_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anthranilate synthase component 1

Short name=AS
Short name=ASI
EC=4.1.3.27
Gene names
Name:trpE
Ordered Locus Names:SSO0893
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Enzyme regulation

Cooperatively feedback inhibited by tryptophan. Ref.4

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.

Subunit structure

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE). Ref.4

Sequence similarities

Belongs to the anthranilate synthase component I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Anthranilate synthase component 1
PRO_0000154132

Regions

Region207 – 2093Tryptophan binding By similarity
Region242 – 2432Substrate binding By similarity
Region391 – 3933Substrate binding By similarity

Sites

Metal binding2691Magnesium By similarity
Metal binding4061Magnesium By similarity
Binding site311Tryptophan By similarity
Binding site3571Substrate By similarity
Binding site3771Substrate By similarity
Binding site3931Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict3371A → R in AAA73379. Ref.1
Sequence conflict3371A → R in CAA90311. Ref.2

Secondary structure

......................................................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06128 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: BD49BD7771ECC6EE

FASTA42147,652
        10         20         30         40         50         60 
MEVHPISEFA SPFEVFKCIE RDFKVAGLLE SIGGPQYKAR YSVIAWSTNG YLKIHDDPVN 

        70         80         90        100        110        120 
ILNGYLKDLK LADIPGLFKG GMIGYISYDA VRFWEKIRDL KPAAEDWPYA EFFTPDNIII 

       130        140        150        160        170        180 
YDHNEGKVYV NADLSSVGGC GDIGEFKVSF YDESLNKNSY ERIVSESLEY IRSGYIFQVV 

       190        200        210        220        230        240 
LSRFYRYIFS GDPLRIYYNL RRINPSPYMF YLKFDEKYLI GSSPELLFRV QDNIVETYPI 

       250        260        270        280        290        300 
AGTRPRGADQ EEDLKLELEL MNSEKDKAEH LMLVDLARND LGKVCVPGTV KVPELMYVEK 

       310        320        330        340        350        360 
YSHVQHIVSK VIGTLKKKYN ALNVLSATFP AGTVSGAPKP MAMNIIETLE EYKRGPYAGA 

       370        380        390        400        410        420 
VGFISADGNA EFAIAIRTAF LNKELLRIHA GAGIVYDSNP ESEYFETEHK LKALKTAIGV 


R 

« Hide

References

« Hide 'large scale' references
[1]"Tryptophan biosynthesis genes trpEGC in the thermoacidophilic archaebacterium Sulfolobus solfataricus."
Tutino M.L., Scarano G., Marino G., Sannia G., Cubellis M.V.
J. Bacteriol. 175:299-302(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 5833 / MT-4.
[2]"Expression of Sulfolobus solfataricus trpE and trpG genes in E. coli."
Tutino M.L., Tosco A., Marino G., Sannia G.
Biochem. Biophys. Res. Commun. 230:306-310(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 5833 / MT-4.
[3]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[4]"The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications."
Knoechel T., Ivens A., Hester G., Gonzalez A., Bauerle R., Wilmanns M., Kirschner K., Jansonius J.N.
Proc. Natl. Acad. Sci. U.S.A. 96:9479-9484(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M98048 Genomic DNA. Translation: AAA73379.1.
Z50014 Genomic DNA. Translation: CAA90311.1.
AE006641 Genomic DNA. Translation: AAK41175.1.
PIRH90239.
JC5323.
RefSeqNP_342385.1. NC_002754.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QDLX-ray2.50A1-421[»]
ProteinModelPortalQ06128.
SMRQ06128. Positions 1-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6202N.
IntActQ06128. 1 interaction.
MINTMINT-102245.
STRING273057.SSO0893.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK41175; AAK41175; SSO0893.
GeneID1455142.
KEGGsso:SSO0893.

Phylogenomic databases

eggNOGCOG0147.
HOGENOMHOG000025142.
KOK01657.
OMAADFAITI.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3603.
SSOL273057:GCH2-849-MONOMER.
UniPathwayUPA00035; UER00040.

Family and domain databases

Gene3D3.60.120.10. 1 hit.
InterProIPR005801. ADC_synthase.
IPR019999. Anth_synth_I_like.
IPR006805. Anth_synth_I_N.
IPR010116. Anthranilate_synth_I_arc_typ.
IPR015890. Chorismate-bd_C.
[Graphical view]
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSPR00095. ANTSNTHASEI.
SUPFAMSSF56322. SSF56322. 1 hit.
TIGRFAMsTIGR01820. TrpE-arch. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ06128.

Entry information

Entry nameTRPE_SULSO
AccessionPrimary (citable) accession number: Q06128
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 20, 2001
Last modified: May 14, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways