HIS51_VIBVY
ID HIS51_VIBVY Reviewed; 204 AA.
AC Q7MLS3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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; OrderedLocusNames=VV1354;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94118.1; -; Genomic_DNA.
DR RefSeq; WP_011080736.1; NC_005139.1.
DR AlphaFoldDB; Q7MLS3; -.
DR SMR; Q7MLS3; -.
DR STRING; 672.VV93_v1c12670; -.
DR EnsemblBacteria; BAC94118; BAC94118; BAC94118.
DR KEGG; vvy:VV1354; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_0_0_6; -.
DR OMA; WVYFVHS; -.
DR OrthoDB; 1726024at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000002675; Chromosome I.
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..204
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 1"
FT /id="PRO_0000152444"
FT DOMAIN 5..204
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 186
FT /evidence="ECO:0000250"
FT ACT_SITE 188
FT /evidence="ECO:0000250"
SQ SEQUENCE 204 AA; 22216 MW; CDB409236FB26517 CRC64;
MTEQKVVIID TGCANVSSVK FAIERLGYDV TISKDPQVVL SADKLFLPGV GTASEAMKNL
EERDLISLVK QVEKPLLGIC LGMQLLGKVS QEKGQKADEL VECLGLCDGE VKLLQTGDLP
LPHMGWNTVS AKAGNPLFKG IEEGEYFYFV HSFAMPVGDY TIAECEYGNS FTAAVQSGNY
YGVQFHPERS SKAGAKLIQN FLEL
