HIS53_VIBVY
ID HIS53_VIBVY Reviewed; 206 AA.
AC Q7MPK8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 3;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit 3;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH 3;
DE AltName: Full=ImGP synthase subunit HisH 3;
DE Short=IGPS subunit HisH 3;
GN Name=hisH3; OrderedLocusNames=VV0355;
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; BAC93119.1; -; Genomic_DNA.
DR RefSeq; WP_011149328.1; NC_005139.1.
DR AlphaFoldDB; Q7MPK8; -.
DR SMR; Q7MPK8; -.
DR EnsemblBacteria; BAC93119; BAC93119; BAC93119.
DR KEGG; vvy:VV0355; -.
DR PATRIC; fig|196600.6.peg.390; -.
DR HOGENOM; CLU_071837_2_0_6; -.
DR OMA; PEKSHRY; -.
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..206
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 3"
FT /id="PRO_0000152446"
FT DOMAIN 1..206
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 188
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 23036 MW; 17B361B1CCC305C6 CRC64;
MITIVDYGLG NIKAFANLYK KLNIELVFAS DVNDLANATK IILPGVGAFD HAMQMLNDSG
MRETLDELVL EKKVPVIGIC VGMQMMADSS EEGQLKGLGW IPGTVKKFKR ESQALESQYP
LPHMGWNSLE IARTSELLLG LDEQKLFYFL HSYYYEPNDK EHVVATANYG FEYACIVNKD
NVYGIQCHPE KSHHNGVALL KSFASL
