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Links from Protein

Items: 9

1.

Anthranilate synthase component I, N terminal region

Anthranilate synthase (EC:4.1.3.27) catalyses the first step in the biosynthesis of tryptophan. Component I catalyses the formation of anthranilate using ammonia and chorismate. The catalytic site lies in the adjacent region, described in the chorismate binding enzyme family (Pfam:PF00425). This region is involved in feedback inhibition by tryptophan [1]. This family also contains a region of Para-aminobenzoate synthase component I (EC 4.1.3.-). [1]. 11371633. 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 MC, Yanofsky C, Mills SE;. Proc Natl Acad Sci U S A 2001;98:6021-6026.. [2]. 11450855. A metabolic node in action: chorismate-utilizing enzymes in. microorganisms.. Dosselaere F, Vanderleyden J;. Crit Rev Microbiol 2001;27:75-131. (from Pfam)

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Date:
2024-08-14
Family Accession:
NF016593.5
Method:
HMM
2.

chorismate-binding protein

This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase. [1]. 11371633. 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 MC, Yanofsky C, Mills SE;. Proc Natl Acad Sci U S A 2001;98:6021-6026.. [2]. 11450855. A metabolic node in action: chorismate-utilizing enzymes in. microorganisms.. Dosselaere F, Vanderleyden J;. Crit Rev Microbiol 2001;27:75-131. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012640.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

aminodeoxychorismate synthase component 1

aminodeoxychorismate synthase component 1 is part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate

Date:
2019-08-06
Family Accession:
11487809
Method:
Sparcle
8.

aminodeoxychorismate synthase component 1

Aminodeoxychorismate synthase subunit PabB; with PabA catalyzes the formation of 4-amino-4-deoxychorismate from chorismate and glutamine in para-aminobenzoate synthesis

Gene:
pabB
GO Terms:
Biological Process:
folic acid-containing compound biosynthetic process (GO:0009396)
Date:
2021-08-12
Family Accession:
NF012009.0
Method:
HMM
9.

aminodeoxychorismate synthase component I

Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824).

Gene:
pabB
GO Terms:
Biological Process:
para-aminobenzoic acid biosynthetic process (GO:0008153)
Biological Process:
folic acid-containing compound biosynthetic process (GO:0009396)
Molecular Function:
4-amino-4-deoxychorismate synthase activity (GO:0046820)
Date:
2021-04-27
Family Accession:
TIGR00553.1
Method:
HMM
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