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 05-SEP-2012, entry version 60. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH; DE EC=2.4.2.-; DE AltName: Full=IGP synthase glutamine amidotransferase subunit; DE AltName: Full=IGP synthase subunit HisH; DE AltName: Full=ImGP synthase subunit HisH; DE Short=IGPS subunit HisH; GN Name=hisH; OrderedLocusNames=SAR2757; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; 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 provides the glutamine CC amidotransferase activity that produces the ammonia necessary to CC HisF for the synthesis of IGP and AICAR (By similarity). CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. 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; YP_042094.1; NC_002952.2. DR ProteinModelPortal; Q6GDC9; -. DR STRING; Q6GDC9; -. DR EnsemblBacteria; EBSTAT00000020740; EBSTAP00000020076; EBSTAG00000020739. DR GeneID; 2860713; -. DR GenomeReviews; BX571856_GR; SAR2757. DR KEGG; sar:SAR2757; -. DR PATRIC; 19549230; VBIStaAur71814_2793. DR eggNOG; COG0118; -. DR HOGENOM; HOG000025030; -. DR KO; K02501; -. DR OMA; RPFFGIC; -. DR ProtClustDB; PRK13142; -. DR BioCyc; SAUR282458:SAR2757-MONOMER; -. DR UniPathway; UPA00031; UER00010. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00278; HisH; 1; -. DR InterPro; IPR017926; GATASE_1. DR InterPro; IPR010139; Imidazole-glycPsynth_HisH. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Histidine biosynthesis; Transferase. FT CHAIN 1 192 Imidazole glycerol phosphate synthase FT subunit HisH. FT /FTId=PRO_0000152425. FT DOMAIN 1 192 Glutamine amidotransferase type-1. FT ACT_SITE 77 77 Nucleophile (By similarity). FT ACT_SITE 169 169 By similarity. FT ACT_SITE 171 171 By similarity. 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 //