HIS5_LEGPN
ID HIS5_LEGPN Reviewed; 213 AA.
AC Q9RDX3;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH;
DE AltName: Full=ImGP synthase subunit HisH;
DE Short=IGPS subunit HisH;
GN Name=hisH;
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43109 / NCTC 12008 / RC1 / Olda / Serogroup 1;
RX PubMed=11043980; DOI=10.1016/s1438-4221(00)80104-6;
RA Lueneberg E., Zetzmann N., Hartmann M., Knirel Y.A., Kooistra O.,
RA Zaehringer U., Helbig J., Frosch M.;
RT "Cloning and functional characterization of a 30 kb gene locus required for
RT lipopolysaccharide biosynthesis in Legionella pneumophila.";
RL Int. J. Med. Microbiol. 290:37-49(2000).
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AJ007311; CAB65214.1; -; Genomic_DNA.
DR RefSeq; WP_010946487.1; NZ_UGOV01000002.1.
DR AlphaFoldDB; Q9RDX3; -.
DR SMR; Q9RDX3; -.
DR STRING; 91892.BIZ52_04070; -.
DR GeneID; 66489937; -.
DR eggNOG; COG0118; Bacteria.
DR OMA; PEKSHRY; -.
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..213
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152383"
FT DOMAIN 3..213
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /evidence="ECO:0000250"
FT ACT_SITE 197
FT /evidence="ECO:0000250"
SQ SEQUENCE 213 AA; 23310 MW; F27CDEFD7C771D7C CRC64;
MSSVSIVDYG VGNLLSVARA FQYFDASVNL VSTPEEIMSA DRLVLPGVGA FEDGMKGLTT
LNFIEPIKQF ARSGKPFLGI CLGMQMMLSR STEFGQHEGL DLIAGEVVSV PSHGVDGQLH
KIPHIGWNEL VSTSEGEDWC HTILKNIPLN SSVYFVHSFM AMPSNPKKRL ADTLYDGQAI
SAVIKDENMY GCQFHPEKSG EVGLSIIQQF LQI
