ID   HIS52_PARMW             Reviewed;         212 AA.
AC   Q7U899;
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 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=SYNW0723;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX569691; CAE07238.1; -; Genomic_DNA.
DR   RefSeq; WP_011127589.1; NC_005070.1.
DR   AlphaFoldDB; Q7U899; -.
DR   SMR; Q7U899; -.
DR   STRING; 84588.SYNW0723; -.
DR   EnsemblBacteria; CAE07238; CAE07238; SYNW0723.
DR   KEGG; syw:SYNW0723; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_2_2_3; -.
DR   OMA; WVYFVHS; -.
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..212
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH
FT                   2"
FT                   /id="PRO_0000152435"
FT   DOMAIN          4..211
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        82
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   212 AA;  22879 MW;  81533ADCE382339A CRC64;
     MGLHLGLIDY GMGNLHSVEK AFNRLGHQPS RVVNPSDLDG CDALVLPGVG SFDPAIDNLQ
     STGLIPDLKR WNEADRPLLG ICLGLQLLFE SSAEGRLEGL GLIKGHVERL PIGAGARIPH
     MGWAPLDLRR ANPMLAAADP LAWVYFVHSY AAVPERPETL AAAASFGSSS VTAMVWQRRL
     GACQFHPEKS SDSGSAMLKR WLDWLQRGAP IG