HIS51_CAMJJ
ID HIS51_CAMJJ Reviewed; 201 AA.
AC A1W0U9; Q939J6; Q9PMY4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 1;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit 1;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH 1;
DE AltName: Full=ImGP synthase subunit HisH 1;
DE Short=IGPS subunit HisH 1;
GN Name=hisH1; Synonyms=hisH-1; OrderedLocusNames=CJJ81176_1332;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11461915; DOI=10.1074/jbc.m104529200;
RA Thibault P., Logan S.M., Kelly J.F., Brisson J.-R., Ewing C.P., Trust T.J.,
RA Guerry P.;
RT "Identification of the carbohydrate moieties and glycosylation motifs in
RT Campylobacter jejuni flagellin.";
RL J. Biol. Chem. 276:34862-34870(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 (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; AY102622; AAK58487.1; -; Genomic_DNA.
DR EMBL; CP000538; EAQ72789.1; -; Genomic_DNA.
DR AlphaFoldDB; A1W0U9; -.
DR SMR; A1W0U9; -.
DR STRING; 354242.CJJ81176_1332; -.
DR PRIDE; A1W0U9; -.
DR EnsemblBacteria; EAQ72789; EAQ72789; CJJ81176_1332.
DR KEGG; cjj:CJJ81176_1332; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_2_0_7; -.
DR OMA; DKVPHMG; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000646; 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..201
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 1"
FT /id="PRO_0000281903"
FT DOMAIN 1..201
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 22733 MW; BC60525EDABC2A3C CRC64;
MIALIDYKAG NLNSVAKAFE KIGAINFIAK NPKDLQKADK LLLPGVGSFK EAMKNLKELG
FIEALKEQVL VQKKPILGIC LGMQLFLERG YEGGVCEGLG FIEGEVVKFE EDLNLKIPHM
GWNELEILKQ DPLYQGINNK SDFYFVHSFY VKCKDEFVSA KAQYGHKFVA SLQKDRIFAT
QFHPEKSQNL GLKLLENFAR L
