HIS52_LEGPH
ID HIS52_LEGPH Reviewed; 199 AA.
AC Q5ZW90;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 2 {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 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00278};
DE AltName: Full=ImGP synthase subunit HisH 2 {ECO:0000255|HAMAP-Rule:MF_00278};
DE Short=IGPS subunit HisH 2 {ECO:0000255|HAMAP-Rule:MF_00278};
GN Name=hisH2 {ECO:0000255|HAMAP-Rule:MF_00278}; OrderedLocusNames=lpg1196;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC AICAR and glutamate. The HisH subunit provides the glutamine
CC amidotransferase activity that produces the ammonia necessary to HisF
CC for the synthesis of IGP and AICAR. {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}.
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DR EMBL; AE017354; AAU27281.1; -; Genomic_DNA.
DR RefSeq; WP_010946929.1; NC_002942.5.
DR RefSeq; YP_095228.1; NC_002942.5.
DR AlphaFoldDB; Q5ZW90; -.
DR SMR; Q5ZW90; -.
DR STRING; 272624.lpg1196; -.
DR MEROPS; C26.965; -.
DR PaxDb; Q5ZW90; -.
DR PRIDE; Q5ZW90; -.
DR EnsemblBacteria; AAU27281; AAU27281; lpg1196.
DR GeneID; 66490374; -.
DR KEGG; lpn:lpg1196; -.
DR PATRIC; fig|272624.6.peg.1258; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_0_0_6; -.
DR OMA; WVYFVHS; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000609; 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-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; Reference proteome.
FT CHAIN 1..199
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 2"
FT /id="PRO_0000231733"
FT DOMAIN 1..199
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 177
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 179
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
SQ SEQUENCE 199 AA; 21936 MW; B7AA33EFF939A9FE CRC64;
MIAVIDVSGN NLTSLTNALI RLGGHFALTH DAEEIQKASH VILPGVGTAR SGMTALQQNG
LIDVLRTLTQ PLLGICLGMQ LLLEYSEEDD IPCLGLIPGV AELLKAERNH PVPHMGWNNL
HWQKTSSLQQ GLNNSDYVYF VHSYALKADN YALARCQYHE EFTAVVKKGN FYGMQFHPEK
SANVGMVLLN NFLSLESTC
