ID F8AK58_METOI Unreviewed; 226 AA.
AC F8AK58;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 29-MAY-2013, entry version 15.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase 1;
DE EC=6.3.5.3;
DE AltName: Full=Phosphoribosylformylglycinamidine synthase I;
GN Name=purQ; OrderedLocusNames=Metok_1462;
OS Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1).
OC Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC Methanococcaceae; Methanothermococcus.
OX NCBI_TaxID=647113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14208 / JCM 11175 / IH1;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M.,
RA Takai K., Miyazaki J., Whitman W., Woyke T.;
RT "Complete sequence of chromosome of Methanothermococcus okinawensis
RT IH1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC -!- SUBUNIT: Heterodimer of two subunits, PurQ and PurL (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; CP002792; AEH07425.1; -; Genomic_DNA.
DR RefSeq; YP_004577203.1; NC_015636.1.
DR ProteinModelPortal; F8AK58; -.
DR EnsemblBacteria; AEH07425; AEH07425; Metok_1462.
DR GeneID; 10773620; -.
DR KEGG; mok:Metok_1462; -.
DR KO; K01952; -.
DR OMA; FPGTNCD; -.
DR BioCyc; MOKI647113:GHB9-1504-MONOMER; -.
DR UniPathway; UPA00074; UER00128.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:HAMAP.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR HAMAP; MF_00421; PurQ; 1; -.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_I.
DR PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase;
KW Ligase; Nucleotide-binding; Purine biosynthesis.
FT DOMAIN 2 226 Glutamine amidotransferase type-1 (By
FT similarity).
FT ACT_SITE 85 85 Nucleophile (By similarity).
FT ACT_SITE 202 202 By similarity.
FT ACT_SITE 204 204 By similarity.
SQ SEQUENCE 226 AA; 24970 MW; 3FBA6AAC56E07817 CRC64;
MDIAVIKFLG TNCDKDVCHT VKLAGGKPEL VWFSETDLSR FNGAVIPGGF SYGDYLRAGA
ISSKTPVING LKKMIDDGKP VLGICNGAQI GLEAGFSYGT LTNNINARFI CKWVYIRVEN
NNTPFTKYYK KGEVLKIPIA HAEGRFYTDE DTLQEMYKKN MVVFKYCDEN GEVTDEVNPN
GSIDNIAGVC NENKNCVLLM PHPERASEKI LGSDDGLNMF KAMISK
//
