ID A0A0V0PTS6_9RHOB Unreviewed; 209 AA. AC A0A0V0PTS6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 13-SEP-2023, entry version 29. 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 ORFNames=AQY21_26430 {ECO:0000313|EMBL:KRW93159.1}; OS Paracoccus sp. MKU1. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Paracoccus. OX NCBI_TaxID=1745182 {ECO:0000313|EMBL:KRW93159.1, ECO:0000313|Proteomes:UP000054373}; RN [1] {ECO:0000313|EMBL:KRW93159.1, ECO:0000313|Proteomes:UP000054373} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MKU1 {ECO:0000313|EMBL:KRW93159.1, RC ECO:0000313|Proteomes:UP000054373}; RA Nasrin Nisha K., Varalakshmi P., Ashokkumar B.; RT "Draft Genome Sequence of Paracoccus sp.MKU1."; RL Submitted (OCT-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KRW93159.1}. 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; LLWQ01000223; KRW93159.1; -; Genomic_DNA. DR RefSeq; WP_058100565.1; NZ_LLWQ01000223.1. DR AlphaFoldDB; A0A0V0PTS6; -. DR STRING; 1745182.AQY21_26430; -. DR EnsemblBacteria; KRW93159; KRW93159; AQY21_26430. DR OrthoDB; 9807137at2; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000054373; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC. 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 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 86 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" FT ACT_SITE 189 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" FT ACT_SITE 191 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1" SQ SEQUENCE 209 AA; 22509 MW; 299768D6BDFDD538 CRC64; MRVALVDYDS GNLHSAEKAF ALMGREAGAE VVVTSDPAEV ARADRIVLPG DGAFPACRAA LDAVPGMVEA LREAVLDRAV PFMGICVGMQ MLAEVGHEYR DTQGLGWIGG EIDAIRAPGL KVPHMGWNDL RVLRPHPLLD GIATGDHAYF VHSWQFRVAD PAHLLATADY GGPVTAVVGR DNIVGTQFHP EKSQAVGLRI IGNFLRWRP //