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 13-FEB-2019, entry version 91. 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}; GN OrderedLocusNames=SAR2757; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; 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., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence 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 CC IGP, AICAR and glutamate. The HisH subunit catalyzes the CC hydrolysis of glutamine to glutamate and ammonia as part of the CC synthesis of IGP and AICAR. The resulting ammonia molecule is CC channeled to the active site of HisF. {ECO:0000255|HAMAP- CC Rule:MF_00278}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1- CC (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + CC D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L- CC glutamate; Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:58475, ChEBI:CHEBI:58525; EC=4.3.2.10; CC Evidence={ECO:0000255|HAMAP-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- CC histidine 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 ProteinModelPortal; Q6GDC9; -. DR SMR; Q6GDC9; -. DR EnsemblBacteria; CAG41732; CAG41732; SAR2757. DR KEGG; sar:SAR2757; -. DR HOGENOM; HOG000025030; -. DR KO; K02501; -. DR OMA; WVYFVHS; -. DR OrthoDB; 1726024at2; -. DR BioCyc; SAUR282458:G1G3O-2998-MONOMER; -. DR UniPathway; UPA00031; UER00010. 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 PANTHER; PTHR42701; PTHR42701; 1. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 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 Imidazole glycerol phosphate synthase FT subunit HisH. FT /FTId=PRO_0000152425. FT DOMAIN 1 192 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00278}. FT ACT_SITE 77 77 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00278}. FT ACT_SITE 169 169 {ECO:0000255|HAMAP-Rule:MF_00278}. FT ACT_SITE 171 171 {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 //