ID A0A0F9ZGZ2_9BACT Unreviewed; 442 AA.
AC A0A0F9ZGZ2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=UR31_C0008G0016 {ECO:0000313|EMBL:KKP43324.1};
OS Parcubacteria group bacterium GW2011_GWA2_33_14.
OC Bacteria.
OX NCBI_TaxID=1618807 {ECO:0000313|EMBL:KKP43324.1, ECO:0000313|Proteomes:UP000034294};
RN [1] {ECO:0000313|EMBL:KKP43324.1, ECO:0000313|Proteomes:UP000034294}
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 -!- 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:KKP43324.1}.
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DR EMBL; LBOS01000008; KKP43324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZGZ2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000034294; 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; 3.30.470.20; 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; 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; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF01071; GARS_A; 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; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKP43324.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 116..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 442 AA; 50493 MW; EA9EA925BCD6E158 CRC64;
MTNEQNGKNN LPIITKELRK FLFVSWESLS GDLALQIKKE GHEVKVYIKS ESDKDVYDGF
LEKIDDWKKY IDWADVLVFD DVGFGEEADK LRKSGKLVVG GSSYTDKLEE NREFGQSEMK
RMGMLTLPHW DFTSHDSALT FIEQNPGRYV YKPSGFVPSD SKGILFLGKD EDGKDIHEII
RSNKKVLDKK IKQFQLQKFA TGVEIAVGAF FNGHDFIYPI NINFEHKKLF PGDIGPFTGE
MGTLMYWSLP NTIFKTTLEK MREEIKKSGY VGYIDINCIA NARGIYPLEW TCRFGYPTIS
IQMEGILSEW GDFLYKIAKG ESVELKTKKG FQIGVICAVP PFPFDDKSEM NIYKDLSIIF
KKPNLDGIHL GDVKLVDENW RIAGETGYAL VVTGSGITVE DARKQVYGRL ENILLQNMFF
RTDIGLGWSE DSDKLQTWGY LY
//
