ID A0A1F6V1Q2_9BACT Unreviewed; 259 AA.
AC A0A1F6V1Q2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase I {ECO:0000313|EMBL:OGI63555.1};
GN ORFNames=A2818_01880 {ECO:0000313|EMBL:OGI63555.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_40_12.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801737 {ECO:0000313|EMBL:OGI63555.1, ECO:0000313|Proteomes:UP000177602};
RN [1] {ECO:0000313|EMBL:OGI63555.1, ECO:0000313|Proteomes:UP000177602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGI63555.1}.
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DR EMBL; MFTN01000001; OGI63555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6V1Q2; -.
DR STRING; 1801737.A2818_01880; -.
DR Proteomes; UP000177602; 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 CDD; cd01740; GATase1_FGAR_AT; 1.
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; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 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 Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 259 AA; 29231 MW; C8042E254E4C2A8D CRC64;
MKNKPKIIIM SGYGLNCEEE TKFAFEWAGG KADIVHINDL IKKPKMLSEY QILAFPGGFS
YGDDTGSGKA YANKFKNHLA KELKAFLSRD TLVIGICNGF QIITNLGILP GALTYNKKGK
YIDRWVDLEV VGQSPWLKGI KKISLPIAHG EGKYVINKKE YENLKKNRQI AFTYAKGEIC
KFQNLEKNPN GSEHDIAGVL AYNGRVLGLM PHPERGMFAH QNPMWPQRKA SFLRGKYKNK
KIEKSGEGLQ IFKNAIKYL
//