ID PUR2_VIBVY Reviewed; 429 AA. AC Q7MGT4; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 2. DT 27-MAR-2024, entry version 124. 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=VV3143; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=196600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJ016; RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L., RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P., RA Lee C.-T., Hor L.-I., Tsai S.-F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen."; RL Genome Res. 13:2577-2587(2003). 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 -!- SEQUENCE CAUTION: CC Sequence=BAC95907.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; BA000037; BAC95907.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_039554945.1; NC_005139.1. DR AlphaFoldDB; Q7MGT4; -. DR SMR; Q7MGT4; -. DR STRING; 672.VV93_v1c28610; -. DR KEGG; vvy:VV3143; -. DR eggNOG; COG0151; Bacteria. DR HOGENOM; CLU_027420_3_1_6; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000002675; Chromosome I. 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..429 FT /note="Phosphoribosylamine--glycine ligase" FT /id="PRO_0000151500" FT DOMAIN 109..316 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT REGION 212..234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 135..196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" SQ SEQUENCE 429 AA; 45744 MW; F2E886F3891C916B CRC64; MNVLIIGSGG REHALGWKAA QNPNVETIFV APGNAGTALE PKLENVNIAV EDIAGLVAFA KEKAIELTIV GPEVPLVLGV VDAFYEAGLP IFGPTQAAAQ LEGSKAFTKD FLARHQIPTA AYANFTDIEP ALAYVREQGA PIVVKADGLA AGKGVIVAMT LEEAEEAIKD MLAGNAFGEA GSRVVIEEFL DGEEASFIVM VDGENVLPMA TSQDHKRVGD KDTGPNTGGM GAYSPAPVVT PEIHNRVMQE VIFPTVRGMA AEGNPYTGFL YAGLMIDKDG TPKVIEYNCR FGDPETQPIM MRMESDLVEL CLAAIDKKLD QVESKWDPRA SIGIVLAAGG YPAAYNKGDV ISGLPQVEIE GEKVFHAGTE NKGGDIVTNG GRVLCATALG NSVSEAQQRA YELAKQIRWD GMFHRNDIGY RAIAREQQK //