ID HIS5_STAAR Reviewed; 192 AA. AC Q6GDC9; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; DE EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_00278}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; DE AltName: Full=ImGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; DE Short=IGPS subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; GN Name=hisH {ECO:0000255|HAMAP-Rule:MF_00278}; OrderedLocusNames=SAR2757; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSA252; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00278}. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP- CC Rule:MF_00278}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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; BX571856; CAG41732.1; -; Genomic_DNA. DR RefSeq; WP_000635613.1; NC_002952.2. DR AlphaFoldDB; Q6GDC9; -. DR SMR; Q6GDC9; -. DR KEGG; sar:SAR2757; -. DR HOGENOM; CLU_071837_2_2_9; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000596; Chromosome. 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-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; Cytoplasm; Glutamine amidotransferase; KW Histidine biosynthesis; Hydrolase; Lyase. FT CHAIN 1..192 FT /note="Imidazole glycerol phosphate synthase subunit HisH" FT /id="PRO_0000152425" FT DOMAIN 1..192 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278" FT ACT_SITE 77 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278" FT ACT_SITE 169 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278" FT ACT_SITE 171 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278" SQ SEQUENCE 192 AA; 21364 MW; 36571BDA89F7D416 CRC64; MIVIVDYGLG NISNVKRAIE HLGYEVVVSN KQNIIDQAET IILPGVGHFK DAMSEIKRLN LDAILAKNTD KKMIGICLGM QLMYEHSDEG DASGLGFIPG NISRIQTEYP VPHLGWNNLV SKHPMLNQDV YFVHSYQAPM SENVIAYAQY GTDIPAIVQF NNYIGIQFHP EKSGTYGLQI LRQAIQGGFI ND //