ID A0A8A3S260_9EURY Unreviewed; 200 AA. AC A0A8A3S260; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 29-MAY-2024, entry version 11. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278}; DE EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_00278}; DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278}; DE AltName: Full=ImGP synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278}; DE Short=IGPS subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278}; GN Name=hisH {ECO:0000256|HAMAP-Rule:MF_00278, GN ECO:0000313|EMBL:QSZ66039.1}; GN ORFNames=RJ40_00235 {ECO:0000313|EMBL:QSZ66039.1}; OS Methanofollis aquaemaris. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanomicrobiaceae; Methanofollis. OX NCBI_TaxID=126734 {ECO:0000313|EMBL:QSZ66039.1}; RN [1] {ECO:0000313|EMBL:QSZ66039.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=N2F9704 {ECO:0000313|EMBL:QSZ66039.1}; RX PubMed=11594621; RA Lai M.C., Chen S.C.; RT "Methanofollis aquaemaris sp. nov., a methanogen isolated from an RT aquaculture fish pond."; RL Int. J. Syst. Evol. Microbiol. 51:1873-1880(2001). RN [2] {ECO:0000313|EMBL:QSZ66039.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=N2F9704 {ECO:0000313|EMBL:QSZ66039.1}; RA Chen S.-C., Chien H.-H., Lai M.-C.; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP-Rule:MF_00278}. 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 Evidence={ECO:0000256|ARBA:ARBA00000619, ECO:0000256|HAMAP- CC Rule:MF_00278}; 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 Evidence={ECO:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP- CC Rule:MF_00278}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC {ECO:0000256|ARBA:ARBA00005091, ECO:0000256|HAMAP-Rule:MF_00278}. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152, CC ECO:0000256|HAMAP-Rule:MF_00278}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP036172; QSZ66039.1; -; Genomic_DNA. DR AlphaFoldDB; A0A8A3S260; -. DR KEGG; maqe:RJ40_00235; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP001042704; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01748; GATase1_IGP_Synthase; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00278; HisH; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010139; Imidazole-glycPsynth_HisH. DR NCBIfam; TIGR01855; IMP_synth_hisH; 1. DR PANTHER; PTHR42701; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1. DR PANTHER; PTHR42701:SF1; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00278}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00278, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP- KW Rule:MF_00278}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00278}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00278}. FT DOMAIN 5..196 FT /note="Glutamine amidotransferase" FT /evidence="ECO:0000259|Pfam:PF00117" FT ACT_SITE 78 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" FT ACT_SITE 181 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" FT ACT_SITE 183 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" SQ SEQUENCE 200 AA; 21444 MW; 1628D1161E928561 CRC64; MKKIVIIDYG LGNLRSVSRG LEKAGASAVI SSDPEAIAAA DALVLPGVGA FRDGMEMLGP IEATVREQAG EVPVLGICLG MQMLMESSEE GGLRAGLGLV PGTVRRFPRV PEMKVPHMGW NTLSVPADEP LFDGVPDGSY VYFVHSYYAS APAEHTMTTT EYIHEFASSV KNGMVYGVQF HPEKSGETGL LILKNFIELD //