ID A0A0V0PTS6_9RHOB Unreviewed; 209 AA. AC A0A0V0PTS6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 14. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278}; DE EC=2.4.2.- {ECO:0000256|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase glutamine amidotransferase subunit {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; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; 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 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. {ECO:0000256|HAMAP- CC Rule:MF_00278, ECO:0000256|SAAS:SAAS00234827}. 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 {ECO:0000256|HAMAP-Rule:MF_00278, ECO:0000256|SAAS:SAAS00371105}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC {ECO:0000256|HAMAP-Rule:MF_00278, ECO:0000256|SAAS:SAAS00371075}. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|HAMAP- CC Rule:MF_00278, ECO:0000256|SAAS:SAAS00371119}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278, CC ECO:0000256|SAAS:SAAS00371204}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KRW93159; KRW93159; AQY21_26430. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000054373; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule. 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 {ECO:0000256|HAMAP-Rule:MF_00278, KW ECO:0000256|SAAS:SAAS00064636}; KW Complete proteome {ECO:0000313|Proteomes:UP000054373}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278, KW ECO:0000256|SAAS:SAAS00448507}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00278, KW ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00448434}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00278, KW ECO:0000256|SAAS:SAAS00064616}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00278, KW ECO:0000256|SAAS:SAAS00064637}. FT DOMAIN 2 209 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT ACT_SITE 86 86 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00278, ECO:0000256|PIRSR:PIRSR000495- FT 1, ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 189 189 {ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1, FT ECO:0000256|PROSITE-ProRule:PRU00605}. FT ACT_SITE 191 191 {ECO:0000256|HAMAP-Rule:MF_00278, FT ECO:0000256|PIRSR:PIRSR000495-1, FT ECO:0000256|PROSITE-ProRule:PRU00605}. 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 //