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Q06129 (TRPG_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. 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 2

Short name=AS
Short name=ASII
EC=4.1.3.27
Alternative name(s):
Anthranilate synthase, GATase component
Anthranilate synthase, glutamine amidotransferase component
Gene names
Name:trpG
Ordered Locus Names:SSO0894
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length195 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 Probable. Ref.3

Catalytic activity

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

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.3

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 195195Anthranilate synthase component 2
PRO_0000056900

Regions

Domain3 – 195193Glutamine amidotransferase type-1
Region54 – 563Glutamine binding By similarity
Region137 – 1382Glutamine binding By similarity

Sites

Active site841For GATase activity By similarity
Active site1751For GATase activity By similarity
Active site1771For GATase activity By similarity
Binding site841Glutamine By similarity
Binding site881Glutamine By similarity

Experimental info

Sequence conflict491I → L in AAA73380. Ref.1
Sequence conflict491I → L in CAA90312. Ref.1

Secondary structure

................................. 195
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06129 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 155B62933E9CD33E

FASTA19521,909
        10         20         30         40         50         60 
MDLTLIIDNY DSFVYNIAQI VGELGSYPIV IRNDEISIKG IERIDPDRII ISPGPGTPEK 

        70         80         90        100        110        120 
REDIGVSLDV IKYLGKRTPI LGVCLGHQAI GYAFGAKIRR ARKVFHGKIS NIILVNNSPL 

       130        140        150        160        170        180 
SLYYGIAKEF KATRYHSLVV DEVHRPLIVD AISAEDNEIM AIHHEEYPIY GVQFHPESVG 

       190 
TSLGYKILYN FLNRV 

« 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]"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.
[3]"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, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M98048 Genomic DNA. Translation: AAA73380.1.
Z50014 Genomic DNA. Translation: CAA90312.1.
AE006641 Genomic DNA. Translation: AAK41176.1.
PIRA99240.
B40635.
RefSeqNP_342386.1. NC_002754.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QDLX-ray2.50B1-195[»]
ProteinModelPortalQ06129.
SMRQ06129. Positions 1-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6203N.
IntActQ06129. 1 interaction.
MINTMINT-102261.
STRING273057.SSO0894.

Protein family/group databases

MEROPSC26.955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK41176; AAK41176; SSO0894.
GeneID1455143.
KEGGsso:SSO0894.

Phylogenomic databases

eggNOGCOG0512.
HOGENOMHOG000025029.
KOK01658.
OMADAYSKED.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3604.
SSOL273057:GCH2-850-MONOMER.
UniPathwayUPA00035; UER00040.

Family and domain databases

Gene3D3.40.50.880. 1 hit.
InterProIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamPF00117. GATase. 1 hit.
[Graphical view]
SUPFAMSSF52317. SSF52317. 1 hit.
TIGRFAMsTIGR00566. trpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ06129.

Entry information

Entry nameTRPG_SULSO
AccessionPrimary (citable) accession number: Q06129
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 1, 2001
Last modified: June 11, 2014
This is version 110 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