ID F3FCK8_PSESX Unreviewed; 196 AA.
AC F3FCK8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864};
DE Flags: Fragment;
GN ORFNames=PSYJA_02524 {ECO:0000313|EMBL:EGH27944.1};
OS Pseudomonas syringae pv. japonica str. M301072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH27944.1, ECO:0000313|Proteomes:UP000004471};
RN [1] {ECO:0000313|EMBL:EGH27944.1, ECO:0000313|Proteomes:UP000004471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EGH27944.1}.
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DR EMBL; AEAH01000110; EGH27944.1; -; Genomic_DNA.
DR AlphaFoldDB; F3FCK8; -.
DR PATRIC; fig|629262.5.peg.416; -.
DR HOGENOM; CLU_1386883_0_0_6; -.
DR Proteomes; UP000004471; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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; IPR020559; PRibGlycinamide_synth_CS.
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 Pfam; PF02843; GARS_C; 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; PS00184; GARS; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EGH27944.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 94..187
FT /note="Phosphoribosylglycinamide synthetase C-domain"
FT /evidence="ECO:0000259|SMART:SM01210"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGH27944.1"
SQ SEQUENCE 196 AA; 21082 MW; 340BE4EE433B0B7C CRC64;
PVVTAEVHQR VMDLVIWPTV RGMADEGNVY TGFLYAGLMI DKAGNPKVIE FNCRFGDPET
QPVMLRLQSS LVLLVEAALA QALDKIEAQW DPRPSLGIVL AAGGYPGDYA KGAVIEGLDA
AAQLEGKIFH AGTALQDERV VTSGGRVLCA TALGDSVGNA QENAYALAAK VDWQGCFYRK
DIGYRAIARE RGEDQE
//
