HIS5_ECOL6
ID HIS5_ECOL6 Reviewed; 196 AA.
AC P60596; P10375;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; OrderedLocusNames=c2550;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81005.1; -; Genomic_DNA.
DR RefSeq; WP_001103560.1; NC_004431.1.
DR AlphaFoldDB; P60596; -.
DR SMR; P60596; -.
DR STRING; 199310.c2550; -.
DR EnsemblBacteria; AAN81005; AAN81005; c2550.
DR GeneID; 60668934; -.
DR KEGG; ecc:c2550; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_0_0_6; -.
DR OMA; WVYFVHS; -.
DR BioCyc; ECOL199310:C2550-MON; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000001410; 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.
FT CHAIN 1..196
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152374"
FT DOMAIN 2..196
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 21653 MW; B75A500ECD50DDD0 CRC64;
MNVVILDTGC ANLNSVKSAI ARHGYEPKVS RDPDVVLLAD KLFLPGVGTA QAAMDQVRER
ELFDLIKACT QPVLGICLGM QLLGRRSEES NGVDLLGIID EDVPKMTDFG LPLPHMGWNR
VYPQAGNRLF QGIEDGAYFY FVHSYAMPVN PWTIAQCNYG EPFTAAVQKD NFYGVQFHPE
RSGAAGAKLL KNFLEM
