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CATH Superfamily 1.20.970.10

Transferase, Pyrimidine Nucleoside Phosphorylase; Chain C

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Transferase, Pyrimidine Nucleoside Phosphorylase; Chain C
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 3165: Anthranilate phosphoribosyltransferase like protei...

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Anthranilate phosphoribosyltransferase. [EC: 2.4.2.18]
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.
  • In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, and EC 5.3.1.24).
 2522 A0A010QRW0 A0A011NDM4 A0A011QVX6 A0A013VPF1 A0A017HDG6 A0A017IHT3 A0A022PIX8 A0A022SZE8 A0A023E575 A0A023RKH3
(2512 more...)
Anthranilate synthase. [EC: 4.1.3.27]
Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
  • In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.2.1.20, and EC 5.3.1.24).
  • The native enzyme in the complex with uses either glutamine or (less efficiently) NH(3).
  • The enzyme separated from the complex uses NH(3) only.
 159 A0A024KUT8 A0A026UZM6 A0A027TMZ9 A0A028E5A4 A0A029KYC4 A0A029PPV9 A0A069XSK5 A0A070DB68 A0A070FJX8 A0A070SMH4
(149 more...)
Indole-3-glycerol-phosphate synthase. [EC: 4.1.1.48]
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C- (3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O.
  • In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.3.27, EC 4.2.1.20, and EC 5.3.1.24).
 2 A0A1F8J181 D8J034
Tryptophan synthase. [EC: 4.2.1.20]
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
  • The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8).
  • The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan.
  • In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24.
  • In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122).
  • That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
 1 A0A0A2VIU5
Phosphoribosylanthranilate isomerase. [EC: 5.3.1.24]
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate.
  • In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27, and EC 4.2.1.20).
 1 A0A1B6BC16