ID PUR2_SYNY3 Reviewed; 419 AA. AC P74232; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 146. 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=slr1159; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-beta-D-ribosylamine + glycine + ATP = N(1)-(5- CC phospho-beta-D-ribosyl)glycinamide + ADP + phosphate + H(+); 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; BA000022; BAA18326.1; -; Genomic_DNA. DR PIR; S75867; S75867. DR AlphaFoldDB; P74232; -. DR SMR; P74232; -. DR FunCoup; P74232; 414. DR STRING; 1148.gene:10499202; -. DR PaxDb; 1148-gene:10499202; -. DR EnsemblBacteria; BAA18326; BAA18326; BAA18326. DR KEGG; syn:slr1159; -. DR eggNOG; COG0151; Bacteria. DR InParanoid; P74232; -. DR PhylomeDB; P74232; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central. 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 FunFam; 3.40.50.20:FF:000006; Phosphoribosylamine--glycine ligase, chloroplastic; 1. DR FunFam; 3.30.470.20:FF:000018; Trifunctional purine biosynthetic protein adenosine-3; 1. DR FunFam; 3.90.600.10:FF:000001; Trifunctional purine biosynthetic protein adenosine-3; 1. 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..419 FT /note="Phosphoribosylamine--glycine ligase" FT /id="PRO_0000151494" FT DOMAIN 109..311 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 135..191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" 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" SQ SEQUENCE 419 AA; 44017 MW; 9701E513A08CF2BC CRC64; MKVAVIGSGG REHTLAWSLV RSPEVSHCYC LPGNGGTAGL PKTENVAIAV DQLGEICEFC QTEKINLVVV GPELPLTLGL TDQLQALGIK VFGPTKAGAE LEASKSWTKQ LLIEAGVPTA FGETFTEPAP AQAYATKMGA PIVVKADGLA AGKGVIVAQT SAEATTAIAE LFDQGFEKIV VEEFLPGEEV SVLALCDGKT VIPLLPAQDH KRIGEGDQGL NTGGMGAYCP APIAPPAVID QVQKQILQPT ANALAKRGID YRGVLYAGLM VSPTGEIKVL EYNCRFGDPE TQAVLPLLAT PLEKVLMACV EQNLEQLGPL QWHSGNAVCV VVAAGGYPGS YRKGDEINGL AEAEAQDVKV FHAGTELKEG KVLTNGGRVL GVTALGKDLS TAIATAYRGV EQIDFDGMYY RRDIGHKAL //