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Information on EC 4.3.2.10 - imidazole glycerol-phosphate synthase and Organism(s) Thermus thermophilus and UniProt Accession Q7SIB9

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.10 imidazole glycerol-phosphate synthase
IUBMB Comments
The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide.
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Thermus thermophilus
UNIPROT: Q7SIB9 not found.
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The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
hishf, hisfh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HIS7
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-
-
-
hisFH
-
-
-
-
IGP synthase
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate-lyase (L-glutamine-hydrolysing; 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide-forming)
The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
show the reaction diagram
the enzyme catalyzes the step in the histidine biosynthetic pathway located at the branch point to de novo purine biosynthesis
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q7SIC0: subunit HisH, Q7SIB9: subunit HisF
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the step in the histidine biosynthetic pathway located at the branch point to de novo purine biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A3P4APB7_THETH
252
0
26967
TrEMBL
-
A0A8D6LRD3_THETH
252
0
26965
TrEMBL
-
A0A1J1EKC8_THETH
252
0
26834
TrEMBL
-
A0A7R7TCJ8_THETH
198
0
21489
TrEMBL
-
A0A3P4AT47_THETH
198
0
21368
TrEMBL
-
A0A510HUD1_THETH
252
0
26994
TrEMBL
-
A0A510HRH3_THETH
198
0
21420
TrEMBL
-
A0A7R7YLE0_THETH
252
0
26862
TrEMBL
-
A0A8D6LF63_THETH
206
0
22302
TrEMBL
-
A0A1J1EH60_THETH
198
0
21509
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of subunit hisF are obtained by the hanging-drop vapor diffusion method at 20°C. The three-dimensional structure of the enzyme from Thermus thermophilus HB8 is determined at 2.3 A resolution, and compared with the structures for the yeast and Thermotoga maritima enzymes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli HB101 is transferred with plasmid, pUC119-hisF or pUC119-hisH. Both proteins are overexpressed in separate cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Omi, R.; Mizuguchi, H.; Goto, M.; Miyahara, I.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K.
Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8 open-closed conformational change and ammonia tunneling
J. Biochem.
132
759-765
2002
Thermus thermophilus (Q7SIC0 AND Q7SIB9)
Manually annotated by BRENDA team