ID B3T9T9_9ZZZZ Unreviewed; 210 AA.
AC B3T9T9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative glutamine amidotransferase class-I {ECO:0000313|EMBL:ABZ09348.1};
GN ORFNames=ALOHA_HF4000APKG7H23ctg3g13 {ECO:0000313|EMBL:ABZ09348.1};
OS uncultured marine microorganism HF4000_APKG7H23.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=455551 {ECO:0000313|EMBL:ABZ09348.1};
RN [1] {ECO:0000313|EMBL:ABZ09348.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA Konstantinidis K.T., Delong E.F.;
RT "Genomic patterns of recombination, clonal divergence and environment in
RT marine microbial populations.";
RL ISME J. 2:1052-1065(2008).
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}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152}.
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DR EMBL; EU016649; ABZ09348.1; -; Genomic_DNA.
DR AlphaFoldDB; B3T9T9; -.
DR UniPathway; UPA00031; UER00010.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 HAMAP; MF_00278; HisH; 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:SF1; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamine amidotransferase {ECO:0000313|EMBL:ABZ09348.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Transferase {ECO:0000313|EMBL:ABZ09348.1}.
FT DOMAIN 5..198
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
SQ SEQUENCE 210 AA; 22444 MW; 17F8A61720A248A1 CRC64;
MDSIVIVDYG AGNLRSVQKA FEHLGHATAI TADPDALIHA PAIVFPGQGA SPPAMAALNS
TGMADAIRDT IRQGKPFFGV CLGLQLLMDW SEEGETPCLG VLSGTVKRLP QGLKVPHIGW
NQVDLQGSSH PVFQGVPQGH FYFVHSYYAD PADPGTVLGT TDYGIQFCSV AARDNLVATQ
FHPEKSGPVG LQIYDNFVRR LVHPGATPVR
//