EzCatDB: D00526
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DB codeD00526
CATH domainDomain 13.60.120.10 : Anthranilate synthase
Domain 23.40.50.880 : Rossmann foldCatalytic domain
E.C.4.1.3.27
CSA1i7q,1qdl
MACiEM0314

CATH domainRelated DB codes (homologues)
3.40.50.880 : Rossmann foldT00021,M00215,T00114
3.60.120.10 : Anthranilate synthaseM00215

Enzyme Name
UniProtKBKEGG

Q06128P00897Q06129P00900
Protein nameAnthranilate synthase component 1Anthranilate synthase component 1Anthranilate synthase component IIAnthranilate synthase component IIanthranilate synthase
anthranilate synthetase
chorismate lyase
chorismate pyruvate-lyase (amino-accepting)
TrpE
SynonymsEC 4.1.3.27
Anthranilate synthase component I
EC 4.1.3.27
Anthranilate synthase component I
EC 4.1.3.27
Glutamine amido-transferase
EC 4.1.3.27
Glutamine amido-transferase
RefSeqNP_342385.1 (Protein)
NC_002754.1 (DNA/RNA sequence)

NP_342386.1 (Protein)
NC_002754.1 (DNA/RNA sequence)

MEROPS

C26.955 (Cysteine)

PfamPF04715 (Anth_synt_I_N)
PF00425 (Chorismate_bind)
[Graphical view]
PF04715 (Anth_synt_I_N)
PF00425 (Chorismate_bind)
[Graphical view]
PF00117 (GATase)
[Graphical view]
PF00117 (GATase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

UniProtKB:Accession NumberQ06128P00897Q06129P00900
Entry nameTRPE_SULSOTRPE_SERMATRPG_SULSOTRPG_SERMA
ActivityChorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
SubunitTetramer of two components I and two components II.Tetramer of two components I and two components II.Tetramer of two components I and two components II.Tetramer of two components I and two components II.
Subcellular location



Cofactor
Binds 1 magnesium ion per subunit.


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00251C00064C00108C00022C00025
CompoundChorismateL-GlutamineAnthranilatePyruvateL-Glutamate
Typecarbohydrate,carboxyl groupamino acids,amide groupamine group,aromatic ring (only carbon atom),carboxyl groupcarbohydrate,carboxyl groupamino acids,carboxyl group
ChEBI17333
18050
58359
30754
32816
16015

PubChem12039
6992086
5961
3734162
227
1060
88747398
44272391
33032

              
1qdlAUnboundUnboundUnboundUnboundUnboundUnbound
1i7qAUnboundUnboundAnalogue:BEZBound:PYRUnboundUnbound
1i7qCUnboundUnboundAnalogue:BEZBound:PYRUnboundUnbound
1i7sAUnboundUnboundUnboundUnboundUnboundUnbound
1i7sCUnboundUnboundUnboundUnboundUnboundUnbound
1qdlBUnboundUnboundUnboundUnboundUnboundUnbound
1i7qBUnboundUnboundUnboundUnboundUnboundBound:ILG
1i7qDUnboundUnboundUnboundUnboundUnboundBound:ILG
1i7sBUnboundUnboundUnboundUnboundUnboundUnbound
1i7sDUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1qdl & Swiss-prot;Q06129
pdbCatalytic residues
         
1qdlA 
1i7qA 
1i7qC 
1i7sA 
1i7sC 
1qdlBCYS 84;HIS 175;GLU 177
1i7qBCYS 85;HIS 172;GLU 174
1i7qDCYS 85;HIS 172;GLU 174
1i7sBCYS 85;HIS 172;GLU 174
1i7sDCYS 85;HIS 172;GLU 174

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.9483-9484
[4]p.6023-6024

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID99380543
PubMed ID10449718
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages9479-84
AuthorsKnochel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN
TitleThe crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Related PDB1qdl
Related UniProtKBQ06128,Q06129
[2]
PubMed ID11237738
JournalBiochem Biophys Res Commun
Year2001
Volume281
Pages858-65
AuthorsTang XF, Ezaki S, Atomi H, Imanaka T
TitleAnthranilate synthase without an LLES motif from a hyperthermophilic archaeon is inhibited by tryptophan.
[3]
PubMed ID11224570
JournalNat Struct Biol
Year2001
Volume8
Pages243-7
AuthorsMorollo AA, Eck MJ
TitleStructure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
Related PDB1i1q
[4]
PubMed ID11371633
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages6021-6
AuthorsSpraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE
TitleThe 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.
Related PDB1i7q,1i7s


createdupdated
2004-06-282009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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