ID PUR2_THEMA Reviewed; 400 AA. AC Q9X0X7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 149. 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=TM_1250; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). 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; AE000512; AAD36325.1; -; Genomic_DNA. DR PIR; D72277; D72277. DR RefSeq; NP_229055.1; NC_000853.1. DR PDB; 1VKZ; X-ray; 2.30 A; A/B=1-400. DR PDBsum; 1VKZ; -. DR AlphaFoldDB; Q9X0X7; -. DR SMR; Q9X0X7; -. DR STRING; 243274.TM_1250; -. DR PaxDb; 243274-THEMA_08085; -. DR DNASU; 898233; -. DR EnsemblBacteria; AAD36325; AAD36325; TM_1250. DR KEGG; tma:TM1250; -. DR PATRIC; fig|243274.18.peg.1564; -. DR eggNOG; COG0151; Bacteria. DR InParanoid; Q9X0X7; -. DR OrthoDB; 9807240at2; -. DR UniPathway; UPA00074; UER00125. DR EvolutionaryTrace; Q9X0X7; -. DR Proteomes; UP000008183; 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..400 FT /note="Phosphoribosylamine--glycine ligase" FT /id="PRO_0000151495" FT DOMAIN 99..303 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 125..186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 273 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT BINDING 275 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 13..24 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 86..93 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 95..104 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 118..125 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 130..138 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 151..162 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 182..192 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:1VKZ" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 230..249 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 255..265 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 268..277 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 282..289 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 291..303 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 314..322 FT /evidence="ECO:0007829|PDB:1VKZ" FT TURN 324..328 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 344..352 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 355..358 FT /evidence="ECO:0007829|PDB:1VKZ" FT STRAND 360..372 FT /evidence="ECO:0007829|PDB:1VKZ" FT HELIX 373..386 FT /evidence="ECO:0007829|PDB:1VKZ" SQ SEQUENCE 400 AA; 44326 MW; 411CE014DD7DE90F CRC64; MKAVRVHILG SGGREHAIGW AFAKQGYEVH FYPGNAGTKR DGTNHPYEGE KTLKAIPEED IVIPGSEEFL VEGVSNWRSN VFGPVKEVAR LEGSKVYAKR FMKKYGIRTA RFEVAETPEE LREKIKKFSP PYVIKADGLA RGKGVLILDS KEETIEKGSK LIIGELIKGV KGPVVIDEFL AGNELSAMAV VNGRNFVILP FVRDYKRLMD GDRGPNTGGM GSWGPVEIPS DTIKKIEELF DKTLWGVEKE GYAYRGFLYL GLMLHDGDPY ILEYNVRLGD PETEVIVTLN PEGFVNAVLE GYRGGKMEPV EPRGFAVDVV LAARGYPDAP EKGKEITLPE EGLIFFAGVA EKDGKLVTNG GRVLHCMGTG ETKEEARRKA YELAEKVHFE GKTYRRDIAL //