ID E1SY33_THESX Unreviewed; 224 AA.
AC E1SY33;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 29-MAY-2013, entry version 20.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase 1;
DE EC=6.3.5.3;
DE AltName: Full=Phosphoribosylformylglycinamidine synthase I;
GN Name=purQ; OrderedLocusNames=Thet_0573;
OS Thermoanaerobacter sp. (strain X513).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=573062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X513;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter sp. X513.";
RL Submitted (SEP-2010) 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; CP002210; ADN54220.1; -; Genomic_DNA.
DR RefSeq; YP_003903511.1; NC_014538.1.
DR ProteinModelPortal; E1SY33; -.
DR EnsemblBacteria; ADN54220; ADN54220; Thet_0573.
DR GeneID; 9760322; -.
DR KEGG; thx:Thet_0573; -.
DR PATRIC; 42445204; VBITheSp37765_0592.
DR HOGENOM; HOG000238240; -.
DR KO; K01952; -.
DR OMA; FPGTNCD; -.
DR BioCyc; TSP573062:GHR1-591-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 2 224 Glutamine amidotransferase type-1 (By
FT similarity).
FT ACT_SITE 86 86 Nucleophile (By similarity).
FT ACT_SITE 194 194 By similarity.
FT ACT_SITE 196 196 By similarity.
SQ SEQUENCE 224 AA; 24851 MW; A51A223EA65ED670 CRC64;
MKFAVIVFPG SNCDVDCYYA VKDGLGEEVE YVWHQEKNLS KYDVIMLPGG FSYGDYLRAG
AIARFSPVME AVREEAEKGK FIIGICNGFQ ILTEAGLLPG ALRKNEGLKF ICNTVSIIVE
NDKTPFTTRL KKGQEILLPI AHGEGNYYVD DKTLKELKEN NQIVFRYKEN INGSVERIAG
VINKKGNVLG MMPHPERAYA PLLGNTDGLY ILGSIMDNFV KGGV
//
