HIS5_CUPPJ
ID HIS5_CUPPJ Reviewed; 217 AA.
AC Q46WL6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
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}; OrderedLocusNames=Reut_A3107;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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:0000255|HAMAP-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; Evidence={ECO:0000255|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:0000255|HAMAP-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: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; CP000090; AAZ62467.1; -; Genomic_DNA.
DR RefSeq; WP_011299250.1; NC_007347.1.
DR AlphaFoldDB; Q46WL6; -.
DR SMR; Q46WL6; -.
DR STRING; 264198.Reut_A3107; -.
DR EnsemblBacteria; AAZ62467; AAZ62467; Reut_A3107.
DR KEGG; reu:Reut_A3107; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_2_0_4; -.
DR OMA; WVYFVHS; -.
DR OrthoDB; 1726024at2; -.
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..217
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000231753"
FT DOMAIN 3..217
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 197
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 199
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
SQ SEQUENCE 217 AA; 23661 MW; D54FF7CF9E857BE9 CRC64;
MTTIAIVDYG VGNLRSVAQA LRAAAPEADV RVVDAPEGIR SADRVVLPGQ GAMPDCMSAL
GASGLQEAVI EAAASKPMFG VCVGEQMLFE SSSEARPGTD KTPCLGLMPG EVIRFELDGM
TQPDGSRYKV PQMGWNRVKQ SRPHPLWDGI PDESWFYFVH SYFVRAQDPA HIAGETEYGV
VFTSAVARDN IFATQFHPEK SAAMGLQLYR NFVHWNP
