HIS51_METMP
ID HIS51_METMP Reviewed; 203 AA.
AC P61782;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 1;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit 1;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH 1;
DE AltName: Full=ImGP synthase subunit HisH 1;
DE Short=IGPS subunit HisH 1;
GN Name=hisH1; Synonyms=hisH; OrderedLocusNames=MMP0256;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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}.
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DR EMBL; BX950229; CAF29812.1; -; Genomic_DNA.
DR RefSeq; WP_011170200.1; NC_005791.1.
DR AlphaFoldDB; P61782; -.
DR SMR; P61782; -.
DR STRING; 267377.MMP0256; -.
DR EnsemblBacteria; CAF29812; CAF29812; MMP0256.
DR GeneID; 2762179; -.
DR KEGG; mmp:MMP0256; -.
DR PATRIC; fig|267377.15.peg.258; -.
DR eggNOG; arCOG00089; Archaea.
DR HOGENOM; CLU_071837_2_2_2; -.
DR OMA; WVYFVHS; -.
DR OrthoDB; 100772at2157; -.
DR BioCyc; MMAR267377:MMP_RS01385-MON; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000590; 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; Reference proteome.
FT CHAIN 1..203
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 1"
FT /id="PRO_0000152461"
FT DOMAIN 1..203
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT ACT_SITE 186
FT /evidence="ECO:0000250"
SQ SEQUENCE 203 AA; 22676 MW; D530607622273F80 CRC64;
MIAIIDYNAG NLRSIEKALE LYTKNIVVTS DPETILSADK LVLPGVGNFG DSMKNISQKT
GDCSLNEIIN KCVQKVPFLG ICLGMQLLLE KSEECPETPG LGVIKGDVIK FKHSEKIPHM
GWNTVNQVQD IPLFEGIANN EYFYFVHSYH VNPSEKDVIS GTTNYGYEFP CILNKKNVYA
TQFHPEKSGK NGLKMIENFV ELI
