DB code: M00215

CATH domain 3.60.120.10 : Anthranilate synthase
3.40.50.880 : Rossmann fold Catalytic domain
1.20.970.- : Transferase, Pyrimidine Nucleoside Phosphorylase; Chain A, domain 3
3.40.1030.- : Pyrimidine Nucleoside Phosphorylase; Chain A, domain 2
E.C. 4.1.3.27 2.4.2.18
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.880 : Rossmann fold D00526 T00021 T00114
3.60.120.10 : Anthranilate synthase D00526

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Includes RefSeq Pfam MEROPS
P00898 Anthranilate synthase component 1
EC 4.1.3.27
Anthranilate synthase component I
None NP_460682.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PF04715 (Anth_synt_I_N)
PF00425 (Chorismate_bind)
[Graphical View]
P00905 Anthranilate synthase component II
EC 4.1.3.27
Glutamine amidotransferase
Anthranilate phosphoribosyltransferase
EC 2.4.2.18
NP_460683.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PF00117 (GATase)
PF02885 (Glycos_trans_3N)
PF00591 (Glycos_transf_3)
[Graphical View] 		C26.960 (Cysteine)

KEGG enzyme name
anthranilate synthase
(EC 4.1.3.27 )
anthranilate synthetase
(EC 4.1.3.27 )
chorismate lyase
(EC 4.1.3.27 )
chorismate pyruvate-lyase (amino-accepting)
(EC 4.1.3.27 )
TrpE
(EC 4.1.3.27 )
anthranilate phosphoribosyltransferase
(EC 2.4.2.18 )
phosphoribosyl-anthranilate pyrophosphorylase
(EC 2.4.2.18 )
PRT
(EC 2.4.2.18 )
anthranilate 5-phosphoribosylpyrophosphatephosphoribosyltransferase
(EC 2.4.2.18 )
anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase
(EC 2.4.2.18 )
phosphoribosylanthranilate pyrophosphorylase
(EC 2.4.2.18 )
phosphoribosylanthranilate transferase
(EC 2.4.2.18 )
anthranilate-PP-ribose-P phosphoribosyltransferase
(EC 2.4.2.18 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00898 TRPE_SALTY Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. Tetramer of two components I and two components II.
P00905 TRPG_SALTY Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- diphosphate. Contains 2 chains with different activities: component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.

KEGG Pathways
Map code Pathways E.C.
MAP00400 Phenylalanine, tyrosine and tryptophan biosynthesis 4.1.3.27 2.4.2.18

Compound table
Substrates Products Intermediates
KEGG-id C00251 C00064 C04302 C00013 C00022 C00025 C00108 C00119
E.C. 4.1.3.27
4.1.3.27
2.4.2.18
2.4.2.18
4.1.3.27
4.1.3.27
4.1.3.27
2.4.2.18
2.4.2.18
Compound Chorismate L-Glutamine N-(5-phospho-D-ribosyl)-anthranilate Diphosphate Pyruvate L-Glutamate Anthranilate 5-Phospho-alpha-D-ribose 1-diphosphate
Type carbohydrate,carboxyl group amino acids,amide group amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,phosphate group/phosphate ion phosphate group/phosphate ion carbohydrate,carboxyl group amino acids,carboxyl group amine group,aromatic ring (only carbon atom),carboxyl group carbohydrate,phosphate group/phosphate ion
ChEBI 17333
 17333
 		18050
 58359
 18050
 58359
 		7091
 7091
 		29888
 29888
 		32816
 32816
 		16015
 16015
 		30754
 30754
 		17111
 17111
PubChem 12039
 12039
 		5961
 6992086
 5961
 6992086
 		440289
 440289
 		1023
 21961011
 1023
 21961011
 		1060
 1060
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
 		227
 3734162
 227
 3734162
 		7339
 7339
1i1qA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1i1qB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
see D00526

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1i1qA
1i1qB CYS 83;HIS 169;GLU 171

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.9483-9484
[4]
p.6023-6024

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 99380543
PubMed ID 10449718
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 9479-84
Authors Knochel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN
Title The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Related PDB 1qdl
Related UniProtKB Q06128 Q06129
[2]
Resource
Comments
Medline ID
PubMed ID 11237738
Journal Biochem Biophys Res Commun
Year 2001
Volume 281
Pages 858-65
Authors Tang XF, Ezaki S, Atomi H, Imanaka T
Title Anthranilate synthase without an LLES motif from a hyperthermophilic archaeon is inhibited by tryptophan.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 11224570
Journal Nat Struct Biol
Year 2001
Volume 8
Pages 243-7
Authors Morollo AA, Eck MJ
Title Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
Related PDB 1i1q
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11371633
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 6021-6
Authors Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE
Title 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.
Related PDB 1i7q 1i7s
Related UniProtKB

Comments
This enzyme is composed of two subunits: component 1 and component 2. The component 1 and the N-terminal domain of the component 2 comprises the enzyme, anthranilate synthase (E.C. 4.1.3.27), whereas the C-terminal domains of the component 2 constitute the enzymes, glutamine amidotransferase and anthranilate phosphoribosyltransferase (E.C. 2.4.2.18).
Although the domain strucutres for anthranilate synthase have been elucidated, the tertiary structures for glutamine amidotransferase and anthranilate phosphoribosyltransferase have not been solved yet. The structures for anthranilate synthase are homologous to those of counterpart enzymes (D00526 in EzCatDB).

Created Updated
2004-06-28 2009-02-26