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P00897 (TRPE_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 103. 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 1

Short name=AS
Short name=ASI
EC=4.1.3.27
Gene names
Name:trpE
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length519 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.1

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit. Ref.1

Enzyme regulation

Feedback inhibited by tryptophan By similarity.

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.1

Sequence similarities

Belongs to the anthranilate synthase component I family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

trpGP009002EBI-1031345,EBI-1031352

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Anthranilate synthase component 1
PRO_0000154111

Regions

Region290 – 2923Tryptophan binding
Region327 – 3282Substrate binding
Region482 – 4843Substrate binding

Sites

Metal binding3601Magnesium
Metal binding4971Magnesium
Binding site391Tryptophan
Binding site4481Substrate
Binding site4681Substrate
Binding site4841Substrate; via amide nitrogen

Experimental info

Sequence conflict502 – 5043ARA → PVP in AAA57308. Ref.4

Secondary structure

..................................................................................... 519
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00897 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: D3B59D47619FB0C1

FASTA51957,658
        10         20         30         40         50         60 
MNTKPQLTLL KVQASYRGDP TTLFHQLCGA RPATLLLESA EINDKQNLQS LLVIDSALPI 

        70         80         90        100        110        120 
TALGHTVSVQ ALTANGPALL PVLDEALPPE VRNQARPNGR ELTFPAIDAV QDEDARLRSL 

       130        140        150        160        170        180 
SVFDALRTLL TLVDSPADER EAVMLGGLFA YDLVAGFENL PAVRQDQRCP DFCFYLAETL 

       190        200        210        220        230        240 
LVLDHQRGSA RLQASVFSEQ ASEAQRLQHR LEQLQAELQQ PPQPIPHQKL ENMQLSCNQS 

       250        260        270        280        290        300 
DEEYGAVVSE LQEAIRQGEI FQVVPSRRFS LPCPAPLGPY QTLKDNNPSP YMFFMQDDDF 

       310        320        330        340        350        360 
TLFGASPESA LKYDAGNRQI EIYPIAGTRP RGRRADGSLD LDLDSRIELE MRTDHKELAE 

       370        380        390        400        410        420 
HLMLVDLARN DLARICQAGS RYVADLTKVD RYSFVMHLVS RVVGTLRADL DVLHAYQACM 

       430        440        450        460        470        480 
NMGTLSGAPK VRAMQLIAAL RSTRRGSYGG RVGYFTAHRH LDTCIVIRSA YVEDGHRTVQ 

       490        500        510 
AGAGVVQDSI RRREADETRN KARAVLRAIA TAHHAKEVF 

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND MAGNESIUM ION, FUNCTION, COFACTOR, SUBUNIT.
[2]"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 1-25.
Strain: SM6.
[3]"The regulatory region of the trp operon of Serratia marcescens."
Miozzari G.F., Yanofsky C.
Nature 276:684-689(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[4]"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] OF 494-519.
Strain: SM6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY027546 Genomic DNA. Translation: AAA57308.2.
PIRA01117.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7QX-ray1.95A/C1-519[»]
1I7SX-ray2.40A/C1-519[»]
ProteinModelPortalP00897.
SMRP00897. Positions 3-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00897. 1 interaction.

Proteomic databases

PRIDEP00897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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.
IPR005257. Anth_synth_I_TrpE.
IPR015890. Chorismate-bd_C.
[Graphical view]
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PIRSFPIRSF001373. TrpE. 1 hit.
PRINTSPR00095. ANTSNTHASEI.
SUPFAMSSF56322. SSF56322. 1 hit.
TIGRFAMsTIGR00565. trpE_proteo. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00897.

Entry information

Entry nameTRPE_SERMA
AccessionPrimary (citable) accession number: P00897
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 14, 2001
Last modified: June 11, 2014
This is version 103 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