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Entry: E8PM93_THESS
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ID   E8PM93_THESS            Unreviewed;       201 AA.
AC   E8PM93;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit {ECO:0000313|EMBL:ADW21248.1};
GN   Name=hisH {ECO:0000313|EMBL:ADW21248.1};
GN   OrderedLocusNames=TSC_c06190 {ECO:0000313|EMBL:ADW21248.1};
OS   Thermus scotoductus (strain ATCC 700910 / SA-01).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21248.1, ECO:0000313|Proteomes:UP000008087};
RN   [1] {ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA   Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA   Gottschalk G., van Heerden E., Litthauer D.;
RT   "The genome sequence of Thermus scotoductus SA-01.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADW21248.1, ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX   PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA   Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA   Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA   Berenguer J., van Heerden E., Litthauer D.;
RT   "Sequence of the hyperplastic genome of the naturally competent Thermus
RT   scotoductus SA-01.";
RL   BMC Genomics 12:577-577(2011).
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         Evidence={ECO:0000256|ARBA:ARBA00000619};
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         Evidence={ECO:0000256|ARBA:ARBA00001062};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000256|ARBA:ARBA00005091}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; CP001962; ADW21248.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8PM93; -.
DR   STRING; 743525.TSC_c06190; -.
DR   MEROPS; C26.965; -.
DR   KEGG; tsc:TSC_c06190; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_2_2_0; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000008087; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:RHEA.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR   NCBIfam; TIGR01855; IMP_synth_hisH; 1.
DR   PANTHER; PTHR42701; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1.
DR   PANTHER; PTHR42701:SF1; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00606,
KW   ECO:0000313|EMBL:ADW21248.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Transferase {ECO:0000313|EMBL:ADW21248.1}.
FT   DOMAIN          4..120
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          164..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  21411 MW;  8D812A7292C23110 CRC64;
     MKALLIDYGS GNLRSAAKAL EAAGFEVSVS SDPRAHLEAS LLVLPGQGHF GQVMQAFRNS
     GFVDRVLAHL ERGLPFLGIC VGMQVLYQES EEAPGVRGLG LVEGVVRRFT QGRVPQMGWN
     RVRFAGAFQE LSGRHFYFAN SYYGPLTPYS LGQGEYEGTP FTALFGQGKP PGPPVPPGKE
     REGGPGLFSP GPPLLPGPLA G
//
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