ID PUR2_STRPN Reviewed; 420 AA. AC Q97T98; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; GN OrderedLocusNames=SP_0051; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., RA Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00138}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; 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:0000255|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP- CC Rule:MF_00138}. 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; AE005672; AAK74240.1; -; Genomic_DNA. DR PIR; G95005; G95005. DR RefSeq; WP_000772229.1; NZ_CP089948.1. DR AlphaFoldDB; Q97T98; -. DR SMR; Q97T98; -. DR PaxDb; 170187-SP_0051; -. DR EnsemblBacteria; AAK74240; AAK74240; SP_0051. DR KEGG; spn:SP_0051; -. DR eggNOG; COG0151; Bacteria. DR PhylomeDB; Q97T98; -. DR BioCyc; SPNE170187:G1FZB-57-MONOMER; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000585; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. 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 HAMAP; MF_00138; GARS; 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; IPR020559; PRibGlycinamide_synth_CS. 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. DR PROSITE; PS00184; GARS; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..420 FT /note="Phosphoribosylamine--glycine ligase" FT /id="PRO_0000151487" FT DOMAIN 108..314 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 134..195 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 284 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 286 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" SQ SEQUENCE 420 AA; 45495 MW; 26738829C6ED917A CRC64; MKLLVVGSGG REHAIAKKLL ESKDVEKVFV APGNDGMTLD GLELVNISIS EHYKLIDFAK TNDVAWTFIG PDDALAAGIV DDFNQAGLKA FGPTRAAAEL EWSKDFAKEI MVKYGVPTAT YGTFSDFEEA KAYIEKHGAP IVVKADGLAL GKGVVVAETV EQAVEAAHEM LLDNKFGDSG ARVVIEEFLE GEEFSLFAFV NGDKFYIMPT AQDHKRAYDG DKGPNTGGMG AYAPVPHLPQ SVVDTAVDTI VKPVLEGVIK EGRPYLGVLY AGLILTADGP KVIEFNARFG DPETQIILPR LTSDFAQNIT DILDSKEPNI MWTDKGVTLG VVVASKGYPL DYERGVELPA KTEGDVITYY AGAKFAENSR ALLSNGGRVY MLVTTADTVK EAQASIYQEL YQQKIEGLFY RTDIGSKAIK //