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HIS5_SACS2
ID   HIS5_SACS2              Reviewed;         199 AA.
AC   O33777;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase glutaminase subunit;
DE            EC=3.5.1.2;
DE   AltName: Full=IGP synthase subunit HisH;
DE   AltName: Full=ImGP synthase subunit HisH;
DE            Short=IGPS subunit HisH;
GN   Name=hisH; OrderedLocusNames=SSO0600; ORFNames=C08_050;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=9209067; DOI=10.1128/jb.179.13.4429-4432.1997;
RA   Charlebois R.L., Sensen C.W., Doolittle W.F., Brown J.R.;
RT   "Evolutionary analysis of the hisCGABdFDEHI gene cluster from the archaeon
RT   Sulfolobus solfataricus P2.";
RL   J. Bacteriol. 179:4429-4432(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of
CC       glutamine to glutamate and ammonia as part of the synthesis of IGP and
CC       AICAR. The resulting ammonia molecule is channeled to the active site
CC       of HisF (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; U82227; AAB63025.1; -; Genomic_DNA.
DR   EMBL; Y18930; CAB57700.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40911.1; -; Genomic_DNA.
DR   PIR; H90206; H90206.
DR   RefSeq; WP_009991119.1; NC_002754.1.
DR   AlphaFoldDB; O33777; -.
DR   SMR; O33777; -.
DR   STRING; 273057.SSO0600; -.
DR   MEROPS; C26.965; -.
DR   EnsemblBacteria; AAK40911; AAK40911; SSO0600.
DR   GeneID; 44129601; -.
DR   KEGG; sso:SSO0600; -.
DR   PATRIC; fig|273057.12.peg.607; -.
DR   eggNOG; arCOG00089; Archaea.
DR   HOGENOM; CLU_071837_2_2_2; -.
DR   InParanoid; O33777; -.
DR   OMA; WVYFVHS; -.
DR   PhylomeDB; O33777; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001974; 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; IBA:GO_Central.
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..199
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH"
FT                   /id="PRO_0000152469"
FT   DOMAIN          2..199
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   199 AA;  22533 MW;  17DB1A86724CE095 CRC64;
     MKALVINYGV GNLYSISSAL KRVGFEVTID NKPRNDYDLI VFPGVGAFSA VAEFILRYRE
     LFNDLRRSGT NFLGVCLGMQ IMFEKGTEGK ESNGLGWFKG IVDKINANVK LPHIGWDLVF
     EVKDSCELTY GLDKKYVYYV HSYVAYPTSG DYVYMKSQYG IEYPALVCDK NVVGTQFHPE
     KSSNTGKIFL ENLKGWIKR
 
 
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