ID A0A1F4XKA3_9BACT Unreviewed; 455 AA.
AC A0A1F4XKA3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255};
DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864};
GN ORFNames=A2V81_03225 {ECO:0000313|EMBL:OGC82135.1};
OS Candidatus Abawacabacteria bacterium RBG_16_42_10.
OC Bacteria; Candidatus Abawacabacteria.
OX NCBI_TaxID=1817814 {ECO:0000313|EMBL:OGC82135.1, ECO:0000313|Proteomes:UP000177614};
RN [1] {ECO:0000313|EMBL:OGC82135.1, ECO:0000313|Proteomes:UP000177614}
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 -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005174}.
CC -!- SIMILARITY: Belongs to the GARS family.
CC {ECO:0000256|ARBA:ARBA00038345}.
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:OGC82135.1}.
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DR EMBL; MEWR01000011; OGC82135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4XKA3; -.
DR STRING; 1817814.A2V81_03225; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000177614; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR InterPro; IPR000115; PRibGlycinamide_synth.
DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR InterPro; IPR020562; PRibGlycinamide_synth_N.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00877; purD; 1.
DR PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01209; GARS_A; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGC82135.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 114..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 455 AA; 50204 MW; 3EBC616E36978FAB CRC64;
MRNTVLVVDG GGRGAVLVDK YAQSEHVDRV LAVPGNDLMK INTDKSVITY PKVKTTSVRE
ILEICVQEKV NLVDVAQDNA VEAGLLDALV EKGIPTVGPT KKAGQIEWDK AWAREFGERH
DIPQPCFKVC SSPQEGFDYI ESQPNQPWFI KASGLAEGKG ALPAKNNEEA KQQIKEMARF
KKAGEVFLIE QWLRGDDDSA GEEFSSYIFS DGKNYKIVGH AQDHKRVNNF DVGENTGGMG
CSTPPLVLEE ELLTKVERTI LDRVINGLHQ EGRPYKGVLY LGGMAVKEKS EQVPYVVEFN
ARWGDPEAEV ILPGLENDLF EVGMAIAEGD LSSIQLKTDS RARVVIAGAS KGYPGNYQNV
KGKQIFGLNE ARKYPGVKIY SAGINEQGGR HFANGGRLFY IVGEGNNAIE ARQKAYEAMS
MVSIDGNNLH YRTDIGWRDV QRLRLQQALS LSSAR
//