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Information on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q9YGB5

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.48 indole-3-glycerol-phosphate synthase
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 4.1.3.27 (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:
Thermococcus kodakarensis
UNIPROT: Q9YGB5
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Word Map
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The enzyme appears in selected viruses and cellular organisms
Synonyms
indole-3-glycerol phosphate synthase, sigps, igp synthase, indoleglycerol phosphate synthase, indole-3-glycerol-phosphate synthase, indoleglycerol phosphate synthetase, prai-ingps, eigps, indole-3-glycerol phosphate synthetase, indole-3-glycerolphosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
indole-3-glycerolphosphate synthase
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eIGPS
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IGPS
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indole-3-glycerol phosphate synthase
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Indole-3-glycerol phosphate synthetase
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Indole-3-glycerol-phosphate synthase
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Indole-3-glycerophosphate synthase
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Indoleglycerol phosphate synthase
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Indoleglycerol phosphate synthetase
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Indoleglycerolphosphate synthetase
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InGP synthase
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InGP synthetase
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InGPS
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Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
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PRAI
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PRAI-InGPS
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sIGPS
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Synthase, indole-3-glycerol phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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SYSTEMATIC NAME
IUBMB Comments
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing; 1-C-(indol-3-yl)glycerol-3-phosphate-forming]
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 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
CAS REGISTRY NUMBER
COMMENTARY hide
9031-60-1
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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
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 95
60°C: about 50% of maximal activity, 95°C: about 45% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significant increase in trp mRNA level is observed in cells grown in medium depleted of L-tryptophan, compared to cells grown in medium supplemented with L-tryptophan, indicating that expression of the gene cluster is regulated at the transcriptional level
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tang, X.; Ezaki, S.; Fujiwara, S.; Takagi, M.; Atomi, H.; Imanaka, T.
The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus kodakaraensis KOD1 is regulated at the transcriptional level and expressed as a single mRNA
Mol. Gen. Genet.
262
815-821
1999
Thermococcus kodakarensis (Q9YGB5), Thermococcus kodakarensis
Manually annotated by BRENDA team