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Information on EC 2.4.2.18 - anthranilate phosphoribosyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WFX5

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.18 anthranilate phosphoribosyltransferase
IUBMB Comments
In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WFX5
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
anthranilate phosphoribosyltransferase, anprt, anthranilate phosphoribosyl transferase, phosphoribosylanthranilate transferase, ssanprt, sanprt, sstrpd, anthranilate prt, trp d, anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
anthranilate phosphoribosyl transferase
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anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
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anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase
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anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase
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-
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anthranilate-PP-ribose-P phosphoribosyltransferase
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-
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phosphoribosyl-anthranilate pyrophosphorylase
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-
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phosphoribosylanthranilate pyrophosphorylase
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-
-
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phosphoribosylanthranilate transferase
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-
-
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phosphoribosyltransferase, anthranilate
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-
-
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PR transferase
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-
-
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PRT
-
-
-
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TrpD
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-alpha-D-ribosyltransferase
In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
CAS REGISTRY NUMBER
COMMENTARY hide
9059-35-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-2-pentenoate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-amino-2-pentenoate + diphosphate
show the reaction diagram
good substrate
-
-
?
2-aminoacrylate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminoacrylate + diphosphate
show the reaction diagram
-
-
-
?
2-aminocrotonate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminocrotonate + diphosphate
show the reaction diagram
good substrate
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
show the reaction diagram
-
-
-
r
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
show the reaction diagram
-
-
-
r
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
anthranilate
2-(2-carboxyphenylamino)-5-(3-phosphonopropoxy)benzoic acid
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2-(2-carboxyphenylamino)-5-(4-phosphonobutoxy)benzoic acid
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2-(2-carboxyphenylamino)-5-(5-phosphonopentyloxy)benzoic acid
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is essential for the virulence of Mycobacterium tuberculosis
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzymes N138A, P180A, R193L, R193A, R194A, and G107P, hanging drop vapor diffusion method, using
in complex with inhibitors, hanging drop vapor diffusion method, using 0.2 M imidazole. malate, pH 7.0, 15% (w/v) PEG 4000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cookson, T.V.; Castell, A.; Bulloch, E.M.; Evans, G.L.; Short, F.L.; Baker, E.N.; Lott, J.S.; Parker, E.J.
Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis
Biochem. J.
461
87-98
2014
Mycobacterium tuberculosis (P9WFX5), Mycobacterium tuberculosis
Manually annotated by BRENDA team
Castell, A.; Short, F.L.; Evans, G.L.; Cookson, T.V.; Bulloch, E.M.; Joseph, D.D.; Lee, C.E.; Parker, E.J.; Baker, E.N.; Lott, J.S.
The substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibition
Biochemistry
52
1776-1787
2013
Mycobacterium tuberculosis (P9WFX5), Mycobacterium tuberculosis
Manually annotated by BRENDA team
Cookson, T.V.; Evans, G.L.; Castell, A.; Baker, E.N.; Lott, J.S.; Parker, E.J.
Structures of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase variants reveal the conformational changes that facilitate delivery of the substrate to the active site
Biochemistry
54
6082-6092
2015
Mycobacterium tuberculosis (P9WFX5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WFX5)
Manually annotated by BRENDA team
Evans, G.L.; Furkert, D.P.; Abermil, N.; Kundu, P.; de Lange, K.M.; Parker, E.J.; Brimble, M.A.; Baker, E.N.; Lott, J.S.
Datasets, processing and refinement details for Mtb-AnPRT inhibitor structures with various space groups
Data Brief
15
1019-1029
2017
Mycobacterium tuberculosis (A5U4M0)
Manually annotated by BRENDA team