DB code: D00526

CATH domain 3.60.120.10 : Anthranilate synthase
3.40.50.880 : Rossmann fold Catalytic domain
E.C. 4.1.3.27
CSA 1i7q 1qdl
M-CSA 1i7q 1qdl
MACiE M0314

CATH domain Related DB codes (homologues)
3.40.50.880 : Rossmann fold T00021 M00215 T00114
3.60.120.10 : Anthranilate synthase M00215

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam MEROPS
Q06128 Anthranilate synthase component 1
EC 4.1.3.27
Anthranilate synthase component I
NP_342385.1 (Protein)
NC_002754.1 (DNA/RNA sequence)
PF04715 (Anth_synt_I_N)
PF00425 (Chorismate_bind)
[Graphical View]
P00897 Anthranilate synthase component 1
EC 4.1.3.27
Anthranilate synthase component I
PF04715 (Anth_synt_I_N)
PF00425 (Chorismate_bind)
[Graphical View]
Q06129 Anthranilate synthase component II
EC 4.1.3.27
Glutamine amido-transferase
NP_342386.1 (Protein)
NC_002754.1 (DNA/RNA sequence)
PF00117 (GATase)
[Graphical View] 		C26.955 (Cysteine)
P00900 Anthranilate synthase component II
EC 4.1.3.27
Glutamine amido-transferase
PF00117 (GATase)
[Graphical View]

KEGG enzyme name
anthranilate synthase
anthranilate synthetase
chorismate lyase
chorismate pyruvate-lyase (amino-accepting)
TrpE

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q06128 TRPE_SULSO Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. Tetramer of two components I and two components II.
P00897 TRPE_SERMA Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. Tetramer of two components I and two components II. Binds 1 magnesium ion per subunit.
Q06129 TRPG_SULSO Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. Tetramer of two components I and two components II.
P00900 TRPG_SERMA Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. Tetramer of two components I and two components II.

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

Compound table
Substrates Products Intermediates
KEGG-id C00251 C00064 C00108 C00022 C00025
E.C.
Compound Chorismate L-Glutamine Anthranilate Pyruvate L-Glutamate
Type carbohydrate,carboxyl group amino acids,amide group amine group,aromatic ring (only carbon atom),carboxyl group carbohydrate,carboxyl group amino acids,carboxyl group
ChEBI 17333
 17333
 		18050
 58359
 18050
 58359
 		30754
 30754
 		32816
 32816
 		16015
 16015
PubChem 12039
 12039
 		5961
 6992086
 5961
 6992086
 		227
 3734162
 227
 3734162
 		1060
 1060
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
1qdlA Unbound Unbound Unbound Unbound Unbound Unbound
1i7qA Unbound Unbound Analogue:BEZ Bound:PYR Unbound Unbound
1i7qC Unbound Unbound Analogue:BEZ Bound:PYR Unbound Unbound
1i7sA Unbound Unbound Unbound Unbound Unbound Unbound
1i7sC Unbound Unbound Unbound Unbound Unbound Unbound
1qdlB Unbound Unbound Unbound Unbound Unbound Unbound
1i7qB Unbound Unbound Unbound Unbound Unbound Bound:ILG
1i7qD Unbound Unbound Unbound Unbound Unbound Bound:ILG
1i7sB Unbound Unbound Unbound Unbound Unbound Unbound
1i7sD Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1qdl & Swiss-prot;Q06129

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1qdlA
1i7qA
1i7qC
1i7sA
1i7sC
1qdlB CYS 84;HIS 175;GLU 177
1i7qB CYS 85;HIS 172;GLU 174
1i7qD CYS 85;HIS 172;GLU 174
1i7sB CYS 85;HIS 172;GLU 174
1i7sD CYS 85;HIS 172;GLU 174

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

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