ID A0A0G0QWH1_9BACT Unreviewed; 450 AA.
AC A0A0G0QWH1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864};
GN ORFNames=UT43_C0019G0005 {ECO:0000313|EMBL:KKR14670.1};
OS Parcubacteria group bacterium GW2011_GWC1_39_29.
OC Bacteria.
OX NCBI_TaxID=1618900 {ECO:0000313|EMBL:KKR14670.1, ECO:0000313|Proteomes:UP000034254};
RN [1] {ECO:0000313|EMBL:KKR14670.1, ECO:0000313|Proteomes:UP000034254}
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 -!- 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:KKR14670.1}.
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DR EMBL; LBWT01000019; KKR14670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0QWH1; -.
DR Proteomes; UP000034254; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKR14670.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 339..439
FT /note="Phosphoribosylglycinamide synthetase C-domain"
FT /evidence="ECO:0000259|SMART:SM01210"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 51312 MW; AB2D3751AD43EF6D CRC64;
MSNGDSKING SNGNGKNSNG HTDKPKYKFL FVSWESLSGD LAWQIQKEGH EVKCFIKNSD
DADVYEGILE RISDWKSFID WADVVVFDDI WFGDQADKLR KAGKAVIGGS SYTDRLEDDR
EFGQTEMQRM GMNILPHWDF SDYDAALQFI LDNPGRYVYK PSLDVASDWK GLLFIGKEED
GKDLYQILSS NKVVLSKKIK SFQLQKFASG VEVGCAAFFN GNDFIMPINI AFEHKRLFPG
EIGPMTGEMG TSMFWCGPNN FFRSTLEKML EPLRASGYVG YIDINCIVNA RGIYPLEFTC
RFGYPTISIQ QEGILSEWGE FFHAIANNQS YDLRTRKGFQ VGVVVATPPF PYEDKSEVEI
YRDTSILFKK PNFEGVHLGD VKIIDGDWKI AGNCGYDLVV TGSGTTMEDA RRMAYNRIDN
IMILNMFYRT DIGMTWPEDR DKMHSWEYIY
//
