ID A0A7L8AHC9_9FLAO Unreviewed; 193 AA. AC A0A7L8AHC9; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 03-MAY-2023, entry version 7. 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:QOD61390.1}; GN ORFNames=H9I45_02775 {ECO:0000313|EMBL:QOD61390.1}; OS Polaribacter haliotis. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae. OX NCBI_TaxID=1888915 {ECO:0000313|EMBL:QOD61390.1, ECO:0000313|Proteomes:UP000516764}; RN [1] {ECO:0000313|EMBL:QOD61390.1, ECO:0000313|Proteomes:UP000516764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 52418 {ECO:0000313|EMBL:QOD61390.1, RC ECO:0000313|Proteomes:UP000516764}; RX PubMed=27902190; RA Kim Y.O., Park I.S., Park S., Nam B.H., Park J.M., Kim D.G., Yoon J.H.; RT "Polaribacter haliotis sp. nov., isolated from the gut of abalone Haliotis RT discus hannai."; RL Int. J. Syst. Evol. Microbiol. 66:5562-5567(2016). 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|HAMAP- CC 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; CP061813; QOD61390.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7L8AHC9; -. DR KEGG; phal:H9I45_02775; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000516764; 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-UniRule. 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 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 PRINTS; PR00097; ANTSNTHASEII. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 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..191 FT /note="Glutamine amidotransferase" FT /evidence="ECO:0000259|Pfam:PF00117" FT ACT_SITE 77 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" FT ACT_SITE 175 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" FT ACT_SITE 177 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" SQ SEQUENCE 193 AA; 21245 MW; 78AEB046EEE272B8 CRC64; MKLIIINYGA GNIKSIQFAF KRLGVDAILS NNIDEIKAAD KVIFPGVGEA SSAMKMLQES GLDKIIPNLK QPVLGICLGM QLMCNSSEEG NTKGLGIFDV DVKKFSNAVK VPQMGWNVIS DLKSDLFTGI KNKEFMYLVH SFYAESCAEA IATTDYEIEY ASALKKDNFY GVQFHPEKSG IEGSKILQNF LNL //