EzCatDB: S00847
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DB codeS00847
RLCP classification5.12.1497400.1 : Elimination
8.121.166300.8 : Isomerization
CATH domainDomain 13.20.20.70 : TIM BarrelCatalytic domain
E.C.5.3.1.24
CSA1nsj

CATH domainRelated DB codes (homologues)
3.20.20.70 : TIM BarrelS00215,S00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
UniProtKBKEGG

P83825Q56320
Protein nameN-(5''-phosphoribosyl)anthranilate isomeraseN-(5''-phosphoribosyl)anthranilate isomerasePhosphoribosylanthranilate isomerase
PRA isomerase
PRAI
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
SynonymsEC 5.3.1.24
PRAI
EC 5.3.1.24
RefSeq
NP_227954.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
PfamPF00697 (PRAI)
[Graphical view]
PF00697 (PRAI)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

UniProtKB:Accession NumberP83825Q56320
Entry nameP83825_THETHTRPF_THEMA
ActivityN-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
SubunitHomodimer.Homodimer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC04302C01302I00057I00058
CompoundN-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate1-[(2-carboxyphenyl)imino]-1-deoxyribulose 5-phosphate1-[(2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate
Typeamine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,phosphate group/phosphate ionamine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,phosphate group/phosphate ion

ChEBI7091
29112


PubChem440289
446894


            
1v5xA00UnboundUnbound  
1v5xB00UnboundUnbound  
1dl3A00UnboundUnbound  
1dl3B00UnboundUnbound  
1lbmA00UnboundAnalogue:137  
1nsjA00UnboundUnbound  

Active-site residues
resource
literature [6]
pdbCatalytic residues
         
1v5xA00CYS 6;ASP 124
1v5xB00CYS 6;ASP 124
1dl3A00CYS 7;ASP 126
1dl3B00CYS 7;ASP 126
1lbmA00CYS 7;ASP 126
1nsjA00CYS 7;ASP 126

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Fig.4,p.12039

references
[1]
PubMed ID8897600
JournalProtein Sci
Year1996
Volume5
Pages2000-8
AuthorsSterner R, Kleemann GR, Szadkowski H, Lustig A, Hennig M, Kirschner K
TitlePhosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer.
[2]
PubMed ID9166771
JournalBiochemistry
Year1997
Volume36
Pages6009-16
AuthorsHennig M, Sterner R, Kirschner K, Jansonius JN
TitleCrystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability.
Related PDB1nsj
[3]
PubMed ID10944186
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages9925-30
AuthorsJurgens C, Strom A, Wegener D, Hettwer S, Wilmanns M, Sterner R
TitleDirected evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.
[4]
PubMed ID10745009
JournalStructure
Year2000
Volume8
Pages265-76
AuthorsThoma R, Hennig M, Sterner R, Kirschner K
TitleStructure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima.
Related PDB1dl3
[5]
PubMed ID11551466
JournalCurr Opin Biotechnol
Year2001
Volume12
Pages376-81
AuthorsHocker B, Jurgens C, Wilmanns M, Sterner R
TitleStability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold.
[6]
PubMed ID12356303
JournalBiochemistry
Year2002
Volume41
Pages12032-42
AuthorsHenn-Sax M, Thoma R, Schmidt S, Hennig M, Kirschner K, Sterner R
TitleTwo (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates.
Related PDB1lbm
[7]
PubMed ID15857781
JournalBiomol Eng
Year2005
Volume22
Pages31-8
AuthorsHocker B
TitleDirected evolution of (betaalpha)(8)-barrel enzymes.
Related PDB1nsj
[8]
PubMed ID15944409
JournalJ Biochem
Year2005
Volume137
Pages569-78
AuthorsTaka J, Ogasahara K, Jeyakanthan J, Kunishima N, Kuroishi C, Sugahara M, Yokoyama S, Yutani K
TitleStabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments.
Related PDB1v5x

comments
According to the literature [6], this enzyme catalyzes the following reactions:
(A) Eliminative double-bond formation; Intramolecular elimination leads to the Schiff-base intermediate formation:
(A1) Asp126 (of 1dl3) acts as a general acid to protonate the franose ring oxygen of the substrate, N-(5-phospho-beta-D-ribosyl)anthranilate (PRA), leading to the cleavage of the covalent bond between the oxygen and the C1' atom of the ring. This reaction yields a Schiff-base intermediate (I00057).
(B) Isomerization; Shift of double-bond position (from N=C-C to N-C=C), forming an enolamine intermediate:
(B1) Cys7 (of 1dl3) acts as a general base to deprotonate the C2' atom of the ribose, leading to the formation of an enolamine intermediate (I00058).
(C) Isomerization; Shift of double-bond position (from C=C-O to C-C=O), giving product:
(C0) This reaction might occur spontaneously, after the dissociation of the enolamine intermediate from the enzyme (see [6]).

createdupdated
2009-07-172010-03-05


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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