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Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase and Organism(s) Streptomyces coelicolor and UniProt Accession P16250

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EC Tree
IUBMB Comments
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].
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This record set is specific for:
Streptomyces coelicolor
UNIPROT: P16250
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Word Map
The taxonomic range for the selected organisms is: Streptomyces coelicolor
The enzyme appears in selected viruses and cellular organisms
Synonyms
prai, phosphoribosyl anthranilate isomerase, phosphoribosylanthranilate isomerase, n-(5'-phosphoribosyl)anthranilate isomerase, pra isomerase, ttprai, trpfctl2, phosphoribosyl isomerase a, trp1p, pftrpf, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoribosyl anthranilate isomerase
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phosphoribosyl isomerase A
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IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
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-
-
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isomerase, phosphoribosylanthranilate
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-
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N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
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-
-
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N-5’-phosphoribosylanthranilate isomerase
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-
-
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PAI
-
-
-
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PRA isomerase
-
-
-
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PRAI
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].
CAS REGISTRY NUMBER
COMMENTARY hide
37259-82-8
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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
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
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
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.0083
N-(5-phospho-beta-D-ribosyl)anthranilate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 12
N-(5-phospho-beta-D-ribosyl)anthranilate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
phosphoribosyl isomerase A takes part in histidine and tryptophan biosynthesis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structure of the PriA mutant R139N is determined to a resolution of 1.95 A
hanging-drop vapour-diffusion method, crystallized using the hanging-drop method in 1.5 M ammonium sulfate and 100 mM sodium citrate pH 4.8. Crystals are obtained up to 0.05 * 0.05 * 0.3 mM size, space group P3(1,2)21, unit cell parameters a = 65.1 A, c = 104.7 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R139N
mutant, used for crystallization, steady-state Michaelis-Menten enzyme kinetic is studied
R19A
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
S81T
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pET-15b
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wright, H.; Barona-Gomez, F.; Hodgson, D.A.; Fueloep, V.
Expression, purification and preliminary crystallographic analysis of phosphoribosyl isomerase (PriA) from Streptomyces coelicolor
Acta Crystallogr. Sect. D
D60
534-536
2004
Streptomyces coelicolor
Manually annotated by BRENDA team
Noda-Garcia, L.; Camacho-Zarco, A.R.; Verdel-Aranda, K.; Wright, H.; Soberon, X.; Fueloep, V.; Barona-Gomez, F.
Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (beta alpha)8 phosphoribosyl isomerase A specific for its phosphoribosyl anthranilate isomerase activity
Protein Sci.
19
535-543
2010
Streptomyces coelicolor (P16250), Streptomyces coelicolor
Manually annotated by BRENDA team