ID HIS5_STAAR STANDARD; PRT; 192 AA. AC Q6GDC9; DT 01-FEB-2005 (Rel. 46, Created) DT 01-FEB-2005 (Rel. 46, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Imidazole glycerol phosphate synthase subunit hisH (EC 2.4.2.-) (IGP DE synthase glutamine amidotransferase subunit) (IGP synthase subunit DE hisH) (ImGP synthase subunit hisH) (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]. 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 PRPP: step 5. CC -!- SUBUNIT: Heterodimer of hisH and hisF (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase 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 HAMAP; MF_00278; -; 1. DR InterPro; IPR011702; GATASE. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR012998; GATASE_TYPE1_AS. DR InterPro; IPR010139; IMP_synth_hisH. DR Pfam; PF00117; GATase; 1. DR PRINTS; PR00096; GATASE. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1. DR PROSITE; PS00442; GATASE_TYPE_I; FALSE_NEG. KW Amino-acid biosynthesis; Complete proteome; KW Glutamine amidotransferase; Histidine biosynthesis; Transferase. FT ACT_SITE 77 77 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 //