HIS52_CAMJE
ID HIS52_CAMJE Reviewed; 195 AA.
AC Q9PM75; Q0P828;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 2;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit 2;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH 2;
DE AltName: Full=ImGP synthase subunit HisH 2;
DE Short=IGPS subunit HisH 2;
GN Name=hisH2; OrderedLocusNames=Cj1600;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35697.1; -; Genomic_DNA.
DR PIR; F81255; F81255.
DR RefSeq; WP_002851270.1; NC_002163.1.
DR RefSeq; YP_002344969.1; NC_002163.1.
DR AlphaFoldDB; Q9PM75; -.
DR SMR; Q9PM75; -.
DR IntAct; Q9PM75; 25.
DR STRING; 192222.Cj1600; -.
DR PaxDb; Q9PM75; -.
DR PRIDE; Q9PM75; -.
DR EnsemblBacteria; CAL35697; CAL35697; Cj1600.
DR GeneID; 904385; -.
DR KEGG; cje:Cj1600; -.
DR PATRIC; fig|192222.6.peg.1576; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_0_0_7; -.
DR OMA; PEKSHRY; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000799; 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..195
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 2"
FT /id="PRO_0000152362"
FT DOMAIN 2..195
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 175
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 21976 MW; 1E03FC5D78262786 CRC64;
MKIIIIDTAC ANLASLKFCL DRLGFNATIS RDLKELESAD KLFLPGVGTA KEAMKNLEQF
NLIDFIQNTK KPLLGICLGM QILGNFSEEL NQETLKLIDF TTQKFKAKEG FTFPHMGWNE
VYSSHALFKG LEGAYFYFVH SYCVGLGKYT IADCEYSQKF SASVMKDNFY GVQFHPERSS
EAGEILISNF IKDIG
