Summary: N-(5'phosphoribosyl)anthranilate (PRA) isomerase
This is the Wikipedia entry entitled "Phosphoribosylanthranilate isomerase". More...
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Phosphoribosylanthranilate isomerase Edit Wikipedia article
3D rendering of Phosophoribosylanthranilate Isomerase
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
crystal structure of mutually generated monomers of dimeric phosphoribosylantranilate isomerase from Thermotoga maritima
In yeast it is encoded by the TRP1 gene.
- N-(5-phospho-beta-D-ribosyl)anthranilate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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
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,
- IGPS:PRAI (indole-3-glycerol-phosphate,
- synthetase/N-5'-phosphoribosylanthranilate isomerase complex), and
- N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase.
Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI). 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.
- 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. doi:10.1016/0076-6879(71)17215-1.
- "TRP1/YDR007W Summary". Saccharomyces genome database. Stanford University.
- 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. doi:10.1016/s0969-2126(00)00106-4. PMID 10745009.
- 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.
- HomoloGene Database. National Center for Biotechnology Information. Blast search for phosphoribosylanthranilate isomerase. http://www.ncbi.nlm.nih.gov/homologene/?term=phosphoribosylanthranilate%20isomerase
N-(5'phosphoribosyl)anthranilate (PRA) isomerase Provide feedback
No Pfam abstract.
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
|Similarity to PfamA using HHSearch:||TMP-TENI|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001240Indole-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].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||phosphoribosylanthranilate isomerase activity (GO:0004640)|
|Biological process||tryptophan metabolic process (GO:0006568)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This large superfamily of TIM barrel enzymes all contain a common phosphate binding site. The phosphate is found in a variety of cofactors and ligands such as FMN [1,2].
The clan contains the following 57 members:Ala_racemase_N ALAD Aldolase AP_endonuc_2 BtpA CdhD CutC DAHP_synth_1 DAHP_synth_2 DeoC DHDPS DHO_dh DHquinase_I DUF1341 DUF2090 DUF556 DUF561 DUF692 DUF993 Dus F_bP_aldolase FMN_dh G3P_antiterm Glu_syn_central Glu_synthase His_biosynth HMGL-like IGPS IMPDH iPGM_N MtrH NanE NAPRTase NeuB NMO OMPdecase Orn_Arg_deC_N Oxidored_FMN PcrB PdxJ PhosphMutase PRAI Pterin_bind QRPTase_C Racemase_4 RhaA Ribul_P_3_epim SOR_SNZ Tagatose_6_P_K ThiG TIM TIM-br_sig_trns TMP-TENI Transaldolase Trp_syntA UvdE UxuA
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_247 (release 2.1)|
|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 build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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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