AC MF_00278; DC Protein; auto TR HAMAP; MF_00278; -; 1; level=0 XX Names: HisH XX ID HIS5 DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH; DE EC=4.3.2.10; DE AltName: Full=IGP synthase glutaminase subunit; DE EC=3.5.1.2; DE AltName: Full=IGP synthase subunit HisH; DE AltName: Full=ImGP synthase subunit HisH; DE Short=IGPS subunit HisH; GN Name=hisH; XX CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, CC AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of CC glutamine to glutamate and ammonia as part of the synthesis of IGP and CC AICAR. The resulting ammonia molecule is channeled to the active site CC of HisF. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5- CC amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D- CC erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate; CC Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475, CC ChEBI:CHEBI:58525; EC=4.3.2.10; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. else CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case XX DR Pfam; PF00117; GATase; 1; trigger=no DR PRINTS; PR00096; GATASE; 1; trigger=no DR NCBIfam; TIGR01855; IMP_synth_hisH; 1; trigger=no DR PROSITE; PS51273; GATASE_TYPE_1; 1; trigger=yes XX case not KW Cytoplasm end case KW Amino-acid biosynthesis KW Histidine biosynthesis KW Hydrolase KW Glutamine amidotransferase KW Lyase XX GO GO:0000107; F:imidazoleglycerol-phosphate synthase activity GO GO:0000105; P:histidine biosynthetic process case GO GO:0009507; C:chloroplast else GO GO:0005737; C:cytoplasm end case XX FT From: HIS5_THEMA (Q9X0C8) FT ACT_SITE 84 FT /note="Nucleophile" FT Condition: C FT ACT_SITE 178 FT Condition: H FT ACT_SITE 180 FT Condition: E XX Size: 186-242; Related: None; Template: P60595; Q9X0C8; Q7SIC0; Scope: Bacteria Archaea Plastid Fusion: Nter: None Cter: None Duplicate: in CAMJE, CAMJR, LEGPA, LEGPH, LEGPL, NITWN, PROMM, PSEAE, PARMW, VIBVY, METMP Plasmid: None Comments: AZOBR seems to lack an internal segment that contains the Cys active site; not shown in alignment XX # Revision 1.49 2023/06/01 //