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| HAMAP annotation rule: MF_00079 |
| Accession |
MF_00079 |
| Dates |
1-JUN-2001 (Created) 25-NOV-2009 (Last updated, Version 30) |
| Protein name |
| RecName: |
Full=ATP phosphoribosyltransferase; Short=ATP-PRTase; Short=ATP-PRT; EC=2.4.2.17; |
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FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of hisG enzymatic activity (By similarity).
CATALYTIC ACTIVITY: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
COFACTOR: Magnesium (By similarity).
ENZYME REGULATION: Feedback inhibited by histidine (By similarity).
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
case <OC:Enterobacteriaceae> or <OC:Mycobacteriaceae>
SUBUNIT: Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme (By similarity).
end case
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
GO:0003879; Molecular function: ATP phosphoribosyltransferase activity.
GO:0000287; Molecular function: magnesium ion binding.
GO:0000105; Biological process: histidine biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
| Size range: |
281-325 amino acids |
| Related UniRules: |
MF_01018 (HIS1) |
| Template: |
P60757 (HIS1_ECOLI); P00499 (HIS1_SALTY); P60759 (HIS1_MYCTU): [Recover all] |
| Scope: |
Bacteria
Archaea |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
None |
| Plasmid encoded: |
None |
| Comments: |
Possible wrong start in HAEIN. Possible wrong start in ARCFU; not shown in alignment and not taken into account in size range. See MF_01018 for the entry relevant to the "short" hisG. |
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