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Database: UniProt
Entry: U3U0T1_9ENTR
LinkDB: U3U0T1_9ENTR
Original site: U3U0T1_9ENTR 
ID   U3U0T1_9ENTR            Unreviewed;       196 AA.
AC   U3U0T1;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE            EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_00278};
DE   AltName: Full=IGP synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_00278};
DE            EC=3.5.1.2 {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=E05_49490 {ECO:0000313|EMBL:BAN99715.1};
OS   Plautia stali symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN99715.1, ECO:0000313|Proteomes:UP000016901};
RN   [1] {ECO:0000313|EMBL:BAN99715.1, ECO:0000313|Proteomes:UP000016901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA   Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT   "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT   lipopolysaccharide.";
RL   Microbiol. Res. 167:48-54(2011).
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:0000256|ARBA:ARBA00025299, ECO:0000256|HAMAP-
CC       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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000619, ECO:0000256|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:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00005091, ECO:0000256|HAMAP-Rule:MF_00278}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC       ECO:0000256|HAMAP-Rule:MF_00278}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278}.
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DR   EMBL; AP012551; BAN99715.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3U0T1; -.
DR   MEROPS; C26.965; -.
DR   KEGG; psts:E05_49490; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_0_0_6; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000016901; 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-UniRule.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00278}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_00278};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00278};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00278};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016901};
KW   Transferase {ECO:0000313|EMBL:BAN99715.1}.
FT   DOMAIN          38..194
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
SQ   SEQUENCE   196 AA;  21284 MW;  B13F8B52664DE190 CRC64;
     MNVVILDTGC ANLSSVKWAI ERLGYTPAVS RDPDVVLRAD KLFLPGVGTA RAAMDQLQER
     ELIELVKACT QPVLGICLGM QLLGRGSDEN GGVSTLGIVD EPVSLMDTQG LPLPHMGWNQ
     ITAQAGNHLF RNIPDGSYFY FVHSYAMPVN AATIAQCDYG LPFTAALQKD NFFGVQFHPE
     RSGKAGAQLL KNFLEM
//
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