ID   HIS51_PARMW             Reviewed;         210 AA.
AC   Q7U924;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=SYNW0435;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(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; BX569690; CAE06950.1; -; Genomic_DNA.
DR   RefSeq; WP_011127309.1; NC_005070.1.
DR   AlphaFoldDB; Q7U924; -.
DR   SMR; Q7U924; -.
DR   STRING; 84588.SYNW0435; -.
DR   EnsemblBacteria; CAE06950; CAE06950; SYNW0435.
DR   KEGG; syw:SYNW0435; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_2_2_3; -.
DR   OMA; DKVPHMG; -.
DR   OrthoDB; 1726024at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001422; 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..210
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH
FT                   1"
FT                   /id="PRO_0000152434"
FT   DOMAIN          3..210
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23115 MW;  3748E17B77FE8309 CRC64;
     MSKIAIVDYG MCNLWSIKSA IQFIGYDSIL TSDPKDILNS SAIILPGVGS FKTGMDNLLS
     LGLSQAIIDA CMFRSIPILG ICLGFQLLCC SSEEPSYTKG LSLLPIQIVP LCRHIDASFV
     LPHVGFTSVY TSKNDPLFKN IANKSDFYFV HSYGAFNVPH DFTTYSYCNY DAKIISSANV
     NHIMGVQFHP EKSQTNGLIL LDNFLSFSNV