HIS5_THET8
ID HIS5_THET8 Reviewed; 200 AA.
AC Q7SIC0; Q5SL63;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=TTHA0430;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HISF, AND SUBUNIT.
RX PubMed=12417026; DOI=10.1093/oxfordjournals.jbchem.a003284;
RA Omi R., Mizuguchi H., Goto M., Miyahara I., Hayashi H., Kagamiyama H.,
RA Hirotsu K.;
RT "Structure of imidazole glycerol phosphate synthase from Thermus
RT thermophilus HB8: open-closed conformational change and ammonia
RT tunneling.";
RL J. Biochem. 132:759-765(2002).
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:0000269|PubMed:12417026}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD70253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP008226; BAD70253.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_143696.1; NC_006461.1.
DR PDB; 1KA9; X-ray; 2.30 A; H=1-200.
DR PDBsum; 1KA9; -.
DR AlphaFoldDB; Q7SIC0; -.
DR SMR; Q7SIC0; -.
DR IntAct; Q7SIC0; 1.
DR STRING; 300852.55771812; -.
DR EnsemblBacteria; BAD70253; BAD70253; BAD70253.
DR KEGG; ttj:TTHA0430; -.
DR PATRIC; fig|300852.9.peg.430; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_2_2_0; -.
DR OMA; WVYFVHS; -.
DR BRENDA; 4.3.2.10; 2305.
DR UniPathway; UPA00031; UER00010.
DR EvolutionaryTrace; Q7SIC0; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Glutamine amidotransferase; Histidine biosynthesis; Hydrolase; Lyase;
KW Reference proteome.
FT CHAIN 1..200
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152439"
FT DOMAIN 4..200
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 178
FT /evidence="ECO:0000305"
FT ACT_SITE 180
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1KA9"
SQ SEQUENCE 200 AA; 21819 MW; 4439C0676CB9056F CRC64;
MRMKALLIDY GSGNLRSAAK ALEAAGFSVA VAQDPKAHEE ADLLVLPGQG HFGQVMRAFQ
ESGFVERVRR HLERGLPFLG ICVGMQVLYE GSEEAPGVRG LGLVPGEVRR FRAGRVPQMG
WNALEFGGAF APLTGRHFYF ANSYYGPLTP YSLGKGEYEG TPFTALLAKE NLLAPQFHPE
KSGKAGLAFL ALARRYFEVL
