ID A0A1G0WW52_9BACT Unreviewed; 352 AA.
AC A0A1G0WW52;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphoribosylamine--glycine ligase {ECO:0000313|EMBL:OGV25662.1};
DE Flags: Fragment;
GN ORFNames=A3J84_01185 {ECO:0000313|EMBL:OGV25662.1};
OS Ignavibacteria bacterium RIFOXYA2_FULL_37_17.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798443 {ECO:0000313|EMBL:OGV25662.1, ECO:0000313|Proteomes:UP000178342};
RN [1] {ECO:0000313|EMBL:OGV25662.1, ECO:0000313|Proteomes:UP000178342}
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 -!- 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 -!- 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:OGV25662.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHAP01000037; OGV25662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WW52; -.
DR Proteomes; UP000178342; 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:InterPro.
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 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; IPR020559; PRibGlycinamide_synth_CS.
DR InterPro; IPR020562; PRibGlycinamide_synth_N.
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; PF02844; GARS_N; 1.
DR SMART; SM01209; GARS_A; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:OGV25662.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 107..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 352
FT /evidence="ECO:0000313|EMBL:OGV25662.1"
SQ SEQUENCE 352 AA; 38283 MW; B2A84DC674E85AE7 CRC64;
MRVLVIGSGG REHALALKIS KSSLLDMLFI MPGNPGTKQV GENVKINPSH GDKTLQFCKD
ERIDLIVIGP EQPLVEGLSD YLRNEGFKVF GPSGKAAEIE AHKSFAKRLM KKYNIPTSDF
AEFQSDEYDN ALSYLKETGY PCVIKADGLA AGKGVLICKN FDQAEKAVKE IFLDKVFGSS
GDKIVIEEFM EGEEASIFAI TDGTDFICLP SSQDHKRIGN KDTGKNTGGM GAYSPAPVVT
NEILSQVENK IIKPTLDGMN KEDCLFTGCL YVGLMITKDG PKVVEYNCRF GDPETQVVLP
LLKGDFLKLL YSSAVGELDK NAVHYEDGCA VCVVAASKGY PDSYQKGFEI AG
//