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 hide
5.3.1.16
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RECOMMENDED NAME
GeneOntology No.
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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histidine metabolism
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Histidine metabolism
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L-histidine biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide aldose-ketose-isomerase
Involved in histidine biosynthesis.
CAS REGISTRY NUMBER
COMMENTARY hide
37318-43-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
HR37Rv
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
A3
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-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
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
?
show the reaction diagram
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enzyme catalyzes the fourth step in histidine biosynthesis
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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
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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-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
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?
N-(5'-Phospho-D-ribosylformimino)-5-amino-1-(5''-phospho-D-ribosyl)-4-imidazolecarboxamide
?
show the reaction diagram
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enzyme catalyzes the fourth step in histidine biosynthesis
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additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 37.9
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
additional information
additional information
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Km-values for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00027 - 32
N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
additional information
additional information
Thermotoga maritima
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turnover-numbers for phosphoribosylanthranilate of mutant enzymes D127V, D127K, D127T, D127G, D127F and D127V/T164H
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Arthrobacter aurescens (strain TC1)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25600
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analytical ultracentrifugation
27400
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analytical ultracentrifugation
28400 - 29500
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equilibrium centrifugation
29000
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high speed equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using the anomalous diffraction signal of the proteins sulfur atoms, enzyme binds a citrate molecule, putative mechanism for the isomerization reaction
hanging drop vapor diffusion method. All four crystal forms display distinct habits and crystallographic parameters
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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10 min, 50% loss of the initial CD signal
95
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10 min, 50% loss of the initial CD signal
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as a his-tagged fusion protein in Saccharomyces cerevisiae
overexpression in Escherichia coli
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the gene complements both hisA and trpF mutants of Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D127F
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mutation generates phosporibosylanthranilate isomerase activity
D127G
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mutation generates phosporibosylanthranilate isomerase activity
D127K
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mutation generates phosporibosylanthranilate isomerase activity
D127N
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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
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mutation generates phosporibosylanthranilate isomerase activity
D127V
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mutation generates phosporibosylanthranilate isomerase activity
D127V/T164H
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mutation generates phosporibosylanthranilate isomerase activity
D51N
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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
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activity with N-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide is immeasurable low
H48A
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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
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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
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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
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