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Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U092

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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:
Pyrococcus furiosus
UNIPROT: Q8U092
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
Synonyms
prai, phosphoribosyl anthranilate isomerase, phosphoribosylanthranilate isomerase, n-(5'-phosphoribosyl)anthranilate isomerase, ttprai, pra isomerase, trpfctl2, trp1p, pftrpf, phosphoribosyl isomerase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
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isomerase, phosphoribosylanthranilate
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N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
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N-5’-phosphoribosylanthranilate isomerase
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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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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
thermodynamically stable and entropically optimized monomeric TIM-barrel enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion experiments at room temperature, crystallizes in space group P6(1), structure is determined at 1.75 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Repo, H.; Oeemig, J.S.; Djupsjbacka, J.; Iwai, H.; Heikinheimo, P.
A monomeric TIM-barrel structure from Pyrococcus furiosus is optimized for extreme temperatures
Acta Crystallogr. Sect. D
68
1479-1487
2012
Pyrococcus furiosus (Q8U092), Pyrococcus furiosus
Manually annotated by BRENDA team