ID PUR2_NEIMA Reviewed; 423 AA. AC Q9JWU6; A1IP84; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 129. 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=NMA0238; OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / OS Z2491). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122587; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15465 / Z2491; RX PubMed=10761919; DOI=10.1038/35006655; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A., RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G., RA Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis RT Z2491."; RL Nature 404:502-506(2000). 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; AL157959; CAM07544.1; -; Genomic_DNA. DR PIR; B82018; B82018. DR RefSeq; WP_002246568.1; NC_003116.1. DR AlphaFoldDB; Q9JWU6; -. DR SMR; Q9JWU6; -. DR EnsemblBacteria; CAM07544; CAM07544; NMA0238. DR KEGG; nma:NMA0238; -. DR HOGENOM; CLU_027420_3_1_4; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000626; 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. FT CHAIN 1..423 FT /note="Phosphoribosylamine--glycine ligase" FT /id="PRO_0000151466" FT DOMAIN 107..314 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 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 423 AA; 44907 MW; 62E3F84C83201963 CRC64; MKLLVIGNGG REHALAWKLA QSPKVETVFV APGNAGTAIE PKLQNIDLTA HQDLIEFCRK ENIVFTVVGP EAPLAAGVVD DFRAAGLKIF GPTQYAAQLE SSKDFAKAFM AKYNIPTAQY QTFENADAAH DYVNQKGAPI VIKADGLAAG KGVIVAMTLD EAHAAIDDML LDNKMGNAGA RVVIEDFLQG EEASFIVMVD GNNVLPMATS QDHKRLLDGD KGLNTGGMGA YSPAPVVTPV VYERAMNEII LPTVAGMKAE GHEFTGFLYA GLMIDQSGAP HTIEFNCRFG DPETQPIMSR LNSDLSDLVE AAIDGKLDSV TAEWSPQTAV GVVLAAQNYP ETPKKGDVIS GLDAANQVGK VFHAGTTANE KGDVLTNGGR VLCVVGLGDN VAQAKAKAYG ALEKISFDGM QYRKDIADKA INR //