ID A0A0G0X6F9_9BACT Unreviewed; 247 AA.
AC A0A0G0X6F9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase 1 {ECO:0000313|EMBL:KKR83212.1};
GN ORFNames=UU29_C0007G0082 {ECO:0000313|EMBL:KKR83212.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWA2_40_9.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618424 {ECO:0000313|EMBL:KKR83212.1, ECO:0000313|Proteomes:UP000034601};
RN [1] {ECO:0000313|EMBL:KKR83212.1, ECO:0000313|Proteomes:UP000034601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKR83212.1}.
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DR EMBL; LCAB01000007; KKR83212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0X6F9; -.
DR PATRIC; fig|1618424.3.peg.489; -.
DR Proteomes; UP000034601; Unassembled WGS sequence.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR NCBIfam; TIGR01737; FGAM_synth_I; 1.
DR PANTHER; PTHR47552; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR PANTHER; PTHR47552:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR Pfam; PF13507; GATase_5; 1.
DR PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 247 AA; 27848 MW; CAA2D1B7B69454A4 CRC64;
MAIQEVRVGF IEKDIRGGEQ PLEVVVVRYP GSNCDFDTLK FFHRGGHNAR FLWHKDTIVP
KADLLVLCGG FAFGDREYER ATGEYRMNPG ARALKSPVME VIDQWAKDER PILGICNGFQ
ILCHAGLLPG KLEHNERGKF FCDDVDVAVE GRSFFNSPDL SGNVYPINIA HGYGRYEVTA
EEYAGLMANK QVFLRYQGFN PNGSVENIAG VCNKDGNIWA MMPHPERIVS LETKRVFLEA
IKKYVRS
//
