ID Q2SMB4_HAHCH Unreviewed; 198 AA.
AC Q2SMB4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 115.
DE SubName: Full=Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit {ECO:0000313|EMBL:ABC28210.1};
DE EC=2.4.2.- {ECO:0000313|EMBL:ABC28210.1};
GN Name=hisH1 {ECO:0000313|EMBL:ABC28210.1};
GN OrderedLocusNames=HCH_01345 {ECO:0000313|EMBL:ABC28210.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC28210.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC28210.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC28210.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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}.
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DR EMBL; CP000155; ABC28210.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2SMB4; -.
DR STRING; 349521.HCH_01345; -.
DR MEROPS; C26.965; -.
DR KEGG; hch:HCH_01345; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_2_0_6; -.
DR OMA; WVYFVHS; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000238; 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 CDD; cd01748; GATase1_IGP_Synthase; 1.
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:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH 1; 1.
DR Pfam; PF00117; GATase; 1.
DR PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW ECO:0000313|EMBL:ABC28210.1};
KW Glycosyltransferase {ECO:0000313|EMBL:ABC28210.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Transferase {ECO:0000313|EMBL:ABC28210.1}.
FT DOMAIN 26..191
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 67
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000495-1,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR000495-1,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR000495-1,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 198 AA; 21956 MW; D2BE8FDD4B5A5019 CRC64;
MSKALQHVAP DARVLVTADP KIIAEADRVL VPGVGAMRDC MGEIVRLGFD RIILDAVASG
RPMLGVCVGM QVLLQRSEEN NGVDCLKVFP GDVKFFGYDL TENGERLKVP HMGWNEVKQT
VDHPMWDGIA DNDRFYFVHS YYAAGDHPEV VAGTCRYGVD FAAAIARDNI FAAQFHPEKS
QHAGLQLLKN FTRWNGRP
//