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9  structures 3604  species 2  interactions 3795  sequences 13  architectures

Family: PRAI (PF00697)

Summary: N-(5'phosphoribosyl)anthranilate (PRA) isomerase

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This is the Wikipedia entry entitled "Phosphoribosylanthranilate isomerase". More...

Phosphoribosylanthranilate isomerase Edit Wikipedia article

phosphoribosylanthranilate isomerase
Phosphoribosylanthranilate isomerase Structure.png
3D rendering of Phosophoribosylanthranilate Isomerase
Identifiers
EC number 5.3.1.24
CAS number 37259-82-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
PRAI
PDB 1dl3 EBI.jpg
crystal structure of mutually generated monomers of dimeric phosphoribosylantranilate isomerase from Thermotoga maritima
Identifiers
Symbol PRAI
Pfam PF00697
Pfam clan CL0036
InterPro IPR001240
SCOP 1pii
SUPERFAMILY 1pii

In enzymology, a phosphoribosylanthranilate isomerase (EC 5.3.1.24) is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan.[1]

This enzyme participates in the phenylalanine, tyrosine and tryptophan biosynthesis pathway, also known as the aromatic amino acid biosynthesis pathway

In yeast it is encoded by the TRP1 gene.[2]

Reaction[edit]

N-(5-phospho-beta-D-ribosyl)anthranilate \rightleftharpoons 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Phosphoribosylanthranilate isomerase Reaction

In other words, this enzyme has one substrate, N-(5-phospho-beta-D-ribosyl)anthranilate, and one product, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. As the name phosphoribosylanthranilate isomerase suggests, it functions as an isomerase, rearranging the parts of the molecule without adding or removing molecules or atoms

Nomenclature[edit]

This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase. Other names in common use include:

  • PRA isomerase,
  • PRAI,
  • IGPS:PRAI (indole-3-glycerol-phosphate,
  • synthetase/N-5'-phosphoribosylanthranilate isomerase complex), and
  • N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase.

Structure[edit]

Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI).[3] The comparison to the known 2.0 A structure of PRAI from Escherichia coli (ePRAI) shows that tPRAI has a TIM-barrel fold, whereas helix alpha5 in ePRAI is replaced by a loop. The subunits of tPRAI associate via the N-terminal faces of their central beta-barrels. Two long, symmetry-related loops that protrude reciprocally into cavities of the other subunit provide for multiple hydrophobic interactions. Moreover, the side chains of the N-terminal methionines and the C-terminal leucines of both subunits are immobilized in a hydrophobic cluster, and the number of salt bridges is increased in tPRAI. These features appear to be mainly responsible for the high thermostability of tPRAI.[4]

Homologous Genes[edit]

This enzyme is found in plant species such as Arabidopsis thaliana and Oryza sativa (Asian Rice). One form of bacterium it is found in Thermotoga maritima.

Phosphoribosylanthranilate isomerase is also found in various forms of fungi such as Kluyveromyces lactis (yeast), Saccharomyces cerevisiae (yeast), and Ashbya gossypii. [5]

References[edit]

  1. ^ Creighton TE, Yanofsky C (1970). "Chorismate to tryptophan (Escherichia coli) - Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase". Methods Enzymol. 17A: 365–380. 
  2. ^ "TRP1/YDR007W Summary". Saccharomyces genome database. Stanford University. 
  3. ^ Thoma R, Hennig M, Sterner R, Kirschner K (March 2000). "Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima". Structure 8 (3): 265–76. PMID 10745009. 
  4. ^ Hennig M, Sterner R, Kirschner K, Jansonius JN (May 1997). "Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability". Biochemistry 36 (20): 6009–16. doi:10.1021/bi962718q. PMID 9166771. 
  5. ^ HomoloGene Database. National Center for Biotechnology Information. Blast search for phosphoribosylanthranilate isomerase. http://www.ncbi.nlm.nih.gov/homologene/?term=phosphoribosylanthranilate%20isomerase

Further reading[edit]

  • Braus GH, Luger K, Paravicini G, Schmidheini T, Kirschner K, Hütter R (June 1988). "The role of the TRP1 gene in yeast tryptophan biosynthesis". J. Biol. Chem. 263 (16): 7868–75. PMID 3286643. 

This article incorporates text from the public domain Pfam and InterPro IPR001240

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N-(5'phosphoribosyl)anthranilate (PRA) isomerase Provide feedback

No Pfam abstract.

Literature references

  1. Wilmanns M, Priestle JP, Niermann T, Jansonius JN; , J Mol Biol 1992;223:477-507.: Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution. PUBMED:1738159 EPMC:1738159


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001240

Indole-3-glycerol phosphate synthase (IGPS) (see INTERPRO) catalyzes the fourth step in the biosynthesis of tryptophan, the ring closure of 1-(2-carboxy-phenylamino)-1-deoxyribulose into indol-3-glycerol-phosphate. In some bacteria, IGPS is a single chain enzyme. In others, such as Escherichia coli, it is the N-terminal domain of a bifunctional enzyme that also catalyzes N-(5-phosphoribosyl)anthranilate isomerase (PRAI) activity, the third step of tryptophan biosynthesis. In fungi, IGPS is the central domain of a trifunctional enzyme that contains a PRAI C-terminal domain and a glutamine amidotransferase (GATase) N-terminal domain (see INTERPRO).

Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI) [PUBMED:10745009]. The comparison to the known 2.0 A structure of PRAI from Escherichia coli (ePRAI) shows that tPRAI has the complete TIM- or (beta alp ha)8-barrel fold, whereas helix alpha5 in ePRAI is replaced by a loop. The subunits of tPRAI associate via the N-terminal faces of their central beta-barrels. Two long, symmetry-related loops that protrude reciprocally into cavities of the other subunit provide for multiple hydrophobic interactions. Moreover, the side chains of the N-terminal methionines and the C-terminal leucines of both subunits are immobilized in a hydrophobic cluster, and the number of salt bridges is increased in tPRAI. These features appear to be mainly responsible for the high thermostability of tPRAI [PUBMED:9166771].

Gene Ontology

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Domain organisation

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  Seed
(23)
Full
(3795)
Representative proteomes NCBI
(2961)
Meta
(2133)
RP15
(323)
RP35
(632)
RP55
(826)
RP75
(968)
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  Seed
(23)
Full
(3795)
Representative proteomes NCBI
(2961)
Meta
(2133)
RP15
(323)
RP35
(632)
RP55
(826)
RP75
(968)
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Seed source: Pfam-B_247 (release 2.1)
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 23
Number in full: 3795
Average length of the domain: 193.90 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 66.13 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.6 20.6
Trusted cut-off 20.6 20.6
Noise cut-off 20.4 20.4
Model length: 197
Family (HMM) version: 17
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Interactions

There are 2 interactions for this family. More...

PRAI IGPS

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PRAI domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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