Information on EC 5.3.1.16 - 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
5.3.1.16
-
RECOMMENDED NAME
GeneOntology No.
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
-
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
Amadori rearrangement
-
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
enzyme catalyzes Amadori rearrangement of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is proposed
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
isomerization
P40545
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
histidine biosynthesis
-
Histidine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide aldose-ketose-isomerase
Involved in histidine biosynthesis.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ketol-isomerase
-
-
-
-
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
P40545
-
BBM II isomerase
-
-
BBM II ketolisomerase
-
-
-
-
BBMII isomerase
Q5TKS8
-
Isomerase, N-(phosphoribosylformimino) aminophosphoribosylimidazolecarboxamide
-
-
-
-
Isomerase, phosphoribosylformiminoaminophosphoribosylimidazolecarboxamide
-
-
-
-
N'-[(5'-phosphoribosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase
-
-
phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxamide isomerase
P40545
-
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37318-43-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
Uniprot
Manually annotated by BRENDA team
Mycobacterium tuberculosis HR37Rv
HR37Rv
-
-
Manually annotated by BRENDA team
Streptomyces coelicolor A3
A3
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
show the reaction diagram
-, O82782
the enzyme catalyzes the fourth step of the His biosynthetic pathway
-
?
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
?
show the reaction diagram
-
-
-
?
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
show the reaction diagram
-
-
-
-
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
N-(5'-Phospho-D-1-ribulosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
show the reaction diagram
-
-
-
-
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
?
show the reaction diagram
-
enzyme catalyzes the fourth step in histidine biosynthesis
-
-
-
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
show the reaction diagram
P40545
ProFAR, aminoaldose
PRFAR, aminoketose
-
r
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24
-
?
additional information
?
-
-
enzyme catalyzes Amadori rearrangements of a thermolabile aminoaldolase into the corresponding aminoketose, reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is poposed
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
enzyme of histidine biosynthesis
-
?
additional information
?
-
-
the enzyme is involved in histidine biosynthesis
-
?
additional information
?
-
-, Q5TKS8
APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
-
-
-
additional information
?
-
Streptomyces coelicolor A3
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24, bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
Mycobacterium tuberculosis HR37Rv
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24, bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
?
show the reaction diagram
-
enzyme catalyzes the fourth step in histidine biosynthesis
-
-
-
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
show the reaction diagram
-, O82782
the enzyme catalyzes the fourth step of the His biosynthetic pathway
-
?
additional information
?
-
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
additional information
?
-
-
enzyme of histidine biosynthesis
-
?
additional information
?
-
-
the enzyme is involved in histidine biosynthesis
-
?
additional information
?
-
-, Q5TKS8
APG10 knockout mutant exhibits embryo lethality, indicating the essential role of the Arabidopsis BBMII isomerase for plant growth
-
-
-
additional information
?
-
Streptomyces coelicolor A3, Mycobacterium tuberculosis HR37Rv
-
bifunctional enzyme with activity of EC 5.3.1.16 and EC 5.3.1.24 has a dual function in both histidine and aromatic amino acid biosynthesis
-
?
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.6
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C or 37C, pH 7.5, wild-type enzyme
1.6
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5
1.8
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37C, pH 7.5
2
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme D127N
2.9
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme H48A
5.6
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme T164A
6.4
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme D51N
37.9
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme R83N
additional information
-
additional information
-
Km-values for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00027
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme D127N
0.018
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme T164A
0.23
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme R83N
0.29
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme D51N
0.38
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, mutant enzyme H48A
0.67
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, wild-type enzyme
1.54
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37C, pH 7.5, wild-type enzyme
2.94
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37C, pH 7.5, wild-type enzyme
4.9
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5
6.08
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
25C, pH 7.5, wild-type enzyme
14.3
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
37C, pH 7.5
32
-
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
-
80C, pH 7.5, wild-type enzyme
additional information
-
additional information
-
turnover-numbers for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25600
-
-
analytical ultracentrifugation
27400
-
-
analytical ultracentrifugation
28400
29500
-
equilibrium centrifugation
29000
-
-
high speed equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 27723, calculation from nucleotide sequence
?
-, O82782
x * 33363, calculation from nucleotide sequence
monomer
-
1 * 25700, equilibrium centrifugation of carboxymethlated enzyme in 8 M urea
monomer
-
1 * 29000, high speed equilibrium centrifugation of the enzyme after complete reduction and alkylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using the anomalous diffraction signal of the proteins sulfur atoms, enzyme binds a citrate molecule, putative mechanism for the isomerization reaction
P40545
hanging drop vapor diffusion method. All four crystal forms display distinct habits and crystallographic parameters
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
10 min, 50% loss of the initial CD signal
95
-
-
10 min, 50% loss of the initial CD signal
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
of the protein
P40545
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the gene complements both hisA and trpF mutants of Escherichia coli
-
as a his-tagged fusion protein in Saccharomyces cerevisiae
P40545
the gene complements both hisA and trpF mutants of Escherichia coli
-
overexpression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D127F
-
mutation generates phosporibosylanthranilate isomerase activity
D127G
-
mutation generates phosporibosylanthranilate isomerase activity
D127K
-
mutation generates phosporibosylanthranilate isomerase activity
D127N
-
turnover number for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2481fold higher than that of the wild-type enzyme. The Km-value for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 3.3fold higher than that of the wild-type enzyme
D127T
-
mutation generates phosporibosylanthranilate isomerase activity
D127V
-
mutation generates phosporibosylanthranilate isomerase activity
D127V/T164H
-
mutation generates phosporibosylanthranilate isomerase activity
D51N
-
turnover number for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.3fold higher than that of the wild-type enzyme. The Km-value for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.4fold higher than that of the wild-type enzyme
D8N
-
activity with N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is immeasurable low
H48A
-
turnover number for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 1.8fold lower than that of the wild-type enzyme. The Km-value for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 4.8fold lower than that of the wild-type enzyme
R83N
-
turnover number for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 2.9fold higher than that of the wild-type enzyme. The Km-value for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 63.2fold higher than that of the wild-type enzyme
T164A
-
turnover number for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 37.2fold higher than that of the wild-type enzyme. The Km-value for N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is 9.3fold higher than that of the wild-type enzyme