AC MF_01018; DC Protein; auto TR HAMAP; MF_01018; -; 1; level=0 XX Names: HisG_Short XX ID HIS1 DE RecName: Full=ATP phosphoribosyltransferase; DE Short=ATP-PRT; DE Short=ATP-PRTase; DE EC=2.4.2.17; GN Name=hisG; XX CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial CC role in the pathway because the rate of histidine biosynthesis seems to CC be controlled primarily by regulation of HisG enzymatic activity. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho- CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, CC ChEBI:CHEBI:73183; EC=2.4.2.17; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. case CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. case CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by CC HisZ. end case CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short CC subfamily. XX DR Pfam; PF01634; HisG; 1; trigger=no DR NCBIfam; TIGR00070; HisG; 1; trigger=no DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1; trigger=no XX KW Amino-acid biosynthesis KW ATP-binding KW Cytoplasm KW Glycosyltransferase KW Histidine biosynthesis KW Nucleotide-binding KW Transferase XX GO GO:0003879; F:ATP phosphoribosyltransferase activity GO GO:0000105; P:histidine biosynthetic process GO GO:0005737; C:cytoplasm XX FT None XX Size: 203-241; Related: MF_00079!; Template: Q02129; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: See MF_00079 for the entry relevant to the "long" hisG XX # Revision 1.37 2023/06/01 //