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P00900 (TRPG_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 93. 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·Interactions·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
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.4

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.4

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

trpEP008972EBI-1031352,EBI-1031345

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 193192Anthranilate synthase component 2
PRO_0000056898

Regions

Domain3 – 193191Glutamine amidotransferase type-1
Region57 – 593Glutamine binding
Region134 – 1352Glutamine binding

Sites

Active site841For GATase activity Probable
Active site1701For GATase activity By similarity
Active site1721For GATase activity By similarity
Binding site841Glutamine
Binding site881Glutamine

Experimental info

Sequence conflict361G → A AA sequence Ref.2
Sequence conflict381E → Q AA sequence Ref.2
Sequence conflict381E → Q AA sequence Ref.3
Sequence conflict451Q → E AA sequence Ref.2
Sequence conflict461H → Q AA sequence Ref.3
Sequence conflict481E → T AA sequence Ref.2
Sequence conflict60 – 623TPS → ASV AA sequence Ref.3
Sequence conflict771Q → R AA sequence Ref.2
Sequence conflict1501S → F AA sequence Ref.2

Secondary structure

.................................. 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00900 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8F53EBFEC7F4524A

FASTA19320,868
        10         20         30         40         50         60 
MADILLLDNV DSFTYNLVDQ LRASGHQVVI YRNQIGAEVI IERLQHMEQP VLMLSPGPGT 

        70         80         90        100        110        120 
PSEAGCMPEL LQRLRGQLPI IGICLGHQAI VEAYGGQVGQ AGEILHGKAS AIAHDGEGMF 

       130        140        150        160        170        180 
AGMANPLPVA RYHSLVGSNI PADLTVNARS GEMVMAVRDD RRRVCGFQFH PESILTTHGA 

       190 
RLLEQTLAWA LAK 

« Hide

References

[1]"Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens."
Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.
J. Mol. Biol. 142:503-517(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primary structure of Serratia marcescens anthranilate synthase component II."
Tso J.Y., Hermodson M.A., Zalkin H.
J. Biol. Chem. 255:1451-1457(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-193.
[3]"Separation of anthranilate synthetase components I and II of Escherichia coli, Salmonella typhimurium, and Serratia marcescens and determination of their amino-terminal sequences by automatic Edman degradation."
Li S.-L., Hanlon J., Yanofsky C.
Biochemistry 13:1736-1744(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-62.
[4]"The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan."
Spraggon G., Kim C., Nguyen-Huu X., Yee M.-C., Yanofsky C., Mills S.E.
Proc. Natl. Acad. Sci. U.S.A. 98:6021-6026(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, ACTIVE SITE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY027546 Genomic DNA. Translation: AAK37409.1.
PIRNNSE2. D92860.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7QX-ray1.95B/D1-193[»]
1I7SX-ray2.40B/D1-193[»]
ProteinModelPortalP00900.
SMRP00900. Positions 2-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00900. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00035; UER00040.

Family and domain databases

InterProIPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamPF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00566. trpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00900.

Entry information

Entry nameTRPG_SERMA
AccessionPrimary (citable) accession number: P00900
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 93 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