HIS52_METMP
ID HIS52_METMP Reviewed; 202 AA.
AC P61783;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 2;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit 2;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH 2;
DE AltName: Full=ImGP synthase subunit HisH 2;
DE Short=IGPS subunit HisH 2;
GN Name=hisH2; OrderedLocusNames=MMP1082;
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; CAF30638.1; -; Genomic_DNA.
DR RefSeq; WP_011171026.1; NC_005791.1.
DR AlphaFoldDB; P61783; -.
DR SMR; P61783; -.
DR STRING; 267377.MMP1082; -.
DR EnsemblBacteria; CAF30638; CAF30638; MMP1082.
DR GeneID; 2761201; -.
DR KEGG; mmp:MMP1082; -.
DR PATRIC; fig|267377.15.peg.1115; -.
DR eggNOG; arCOG00089; Archaea.
DR HOGENOM; CLU_071837_2_0_2; -.
DR OMA; DKVPHMG; -.
DR OrthoDB; 100772at2157; -.
DR BioCyc; MMAR267377:MMP_RS05595-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..202
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 2"
FT /id="PRO_0000152462"
FT DOMAIN 1..202
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 22797 MW; 23006D55D41DFDC8 CRC64;
MIAIIDYGMG NVGSIKNMIA KIGFDAIITN DPELISKATK LILPGVGSFD SGMTNLKELG
LIDILNKKVV QEKTPLLGIC LGMHLLTNSS EEGRLKGLGF INAKTVKFKL SNKFKIPHMG
WNYVKFSIKN KLSDNLIENS RFYFVHSYYV ICEDKKNILM TTEYENEFTS AVSKDNIYGV
QFHPEKSHKF GMKLMENFIK QA
