ID PUR2_AQUAE Reviewed; 424 AA. AC O66949; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 136. 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}; OrderedLocusNames=aq_742; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). 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; AE000657; AAC06907.1; -; Genomic_DNA. DR PIR; B70365; B70365. DR RefSeq; NP_213510.1; NC_000918.1. DR RefSeq; WP_010880448.1; NC_000918.1. DR PDB; 2YW2; X-ray; 1.80 A; A/B=1-424. DR PDB; 2YYA; X-ray; 2.40 A; A/B=1-424. DR PDBsum; 2YW2; -. DR PDBsum; 2YYA; -. DR AlphaFoldDB; O66949; -. DR SMR; O66949; -. DR STRING; 224324.aq_742; -. DR EnsemblBacteria; AAC06907; AAC06907; aq_742. DR KEGG; aae:aq_742; -. DR PATRIC; fig|224324.8.peg.593; -. DR eggNOG; COG0151; Bacteria. DR HOGENOM; CLU_027420_3_1_0; -. DR InParanoid; O66949; -. DR OrthoDB; 9807240at2; -. DR BRENDA; 6.3.4.13; 396. DR UniPathway; UPA00074; UER00125. DR EvolutionaryTrace; O66949; -. DR Proteomes; UP000000798; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..424 FT /note="Phosphoribosylamine--glycine ligase" FT /id="PRO_0000151434" FT DOMAIN 107..313 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 133..194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 283 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT STRAND 2..9 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 10..19 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 26..32 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 51..61 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 78..84 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:2YW2" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 98..101 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 103..112 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 126..136 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 159..170 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 190..200 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 203..206 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:2YW2" FT TURN 218..220 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 228..233 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 239..248 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 250..260 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 265..275 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 278..287 FT /evidence="ECO:0007829|PDB:2YW2" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 293..298 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 304..312 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 323..332 FT /evidence="ECO:0007829|PDB:2YW2" FT TURN 334..337 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 349..353 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 358..368 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 371..374 FT /evidence="ECO:0007829|PDB:2YW2" FT STRAND 376..388 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 389..400 FT /evidence="ECO:0007829|PDB:2YW2" FT TURN 414..418 FT /evidence="ECO:0007829|PDB:2YW2" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:2YW2" SQ SEQUENCE 424 AA; 47430 MW; 06EB10D23A68E2FD CRC64; MKVLVVGNGG REHAIAWKVA QSPLVKELYV AKGNAGIWEI AKRVDISPTD VEKLAEFAKN EGVDFTIVGP EAPLVEGIVD EFEKRGLKIF GPNKEAAKLE GSKAFAKTFM KKYGIPTARY EVFTDFEKAK EYVEKVGAPI VVKADGLAAG KGAVVCETVE KAIETLDRFL NKKIFGKSSE RVVIEEFLEG EEASYIVMIN GDRYVPLPTS QDHKRLLDED KGPNTGGMGA YSPTPVINEE VEKRIREEIV ERVIKGLKEE GIYYRGFLYA GLMITKEGPK VLEFNVRLGD PEAQPILMRV KNDFLETLLN FYEGKDVHIK EDERYALDVV LASRGYPEKP ETGKIIHGLD YLKSMEDVVV FHAGTKKEGN FTVTSGGRVL NVCAYGKTLK EAKERAYEAI RYVCFEGMHY RKDIGDKAFK YLSE //