HIS5_CYAM1
ID HIS5_CYAM1 Reviewed; 206 AA.
AC Q85FY4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit hisH;
DE EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_00278};
DE AltName: Full=IGP synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_00278};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00278};
DE AltName: Full=IGP synthase subunit hisH;
DE AltName: Full=ImGP synthase subunit hisH;
DE Short=IGPS subunit hisH;
GN Name=hisH {ECO:0000255|HAMAP-Rule:MF_00278};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
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. {ECO:0000255|HAMAP-Rule:MF_00278}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00278};
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:0000255|HAMAP-Rule:MF_00278};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC {ECO:0000255|HAMAP-Rule:MF_00278}.
CC -!- SUBUNIT: Heterodimer of hisH and hisF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR EMBL; AB002583; BAC76209.1; -; Genomic_DNA.
DR RefSeq; NP_849047.1; NC_004799.1.
DR AlphaFoldDB; Q85FY4; -.
DR SMR; Q85FY4; -.
DR STRING; 45157.CMV138CT; -.
DR EnsemblPlants; CMV138CT; CMV138CT; CMV138C.
DR GeneID; 844892; -.
DR Gramene; CMV138CT; CMV138CT; CMV138C.
DR KEGG; cme:CymeCp115; -.
DR eggNOG; KOG0623; Eukaryota.
DR HOGENOM; CLU_071837_2_2_1; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000007014; Chloroplast.
DR GO; GO:0009507; C:chloroplast; 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; Chloroplast; Glutamine amidotransferase;
KW Histidine biosynthesis; Hydrolase; Lyase; Plastid; Reference proteome.
FT CHAIN 1..206
FT /note="Imidazole glycerol phosphate synthase subunit hisH"
FT /id="PRO_0000152472"
FT DOMAIN 2..206
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 184
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 186
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
SQ SEQUENCE 206 AA; 23294 MW; E54174354A3B8687 CRC64;
MKVGLVDYSM GNMHSVSRAI QQANQQVCVV RSESELAQVH ILVVPGVGHF DLAMKKLEQK
GLRTGIAKWI AKGNPYIGIC LGMHILFETS EEGKEEGLGV YKEQVKRLPV KVIPHMGWNR
LECQNSECQN SEWVNWKAWP NAWAYFVHSY GVMASSQACA TTTYEKIQMV AAIEKDNCFA
MQFHPEKSGE FGLWLWREVM KKAASL
