ID Q5E256_VIBF1 Unreviewed; 430 AA. AC Q5E256; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 02-NOV-2016, entry version 96. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000256|HAMAP-Rule:MF_00138, GN ECO:0000313|EMBL:AAW86890.1}; GN OrderedLocusNames=VF_2395 {ECO:0000313|EMBL:AAW86890.1}; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86890.1, ECO:0000313|Proteomes:UP000000537}; RN [1] {ECO:0000313|EMBL:AAW86890.1, ECO:0000313|Proteomes:UP000000537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537}; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC {ECO:0000256|HAMAP-Rule:MF_00138}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00138}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00138}; CC Note=Binds 1 magnesium or manganese ion per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00138}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP- CC Rule:MF_00138}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|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; CP000020; AAW86890.1; -; Genomic_DNA. DR RefSeq; WP_011262779.1; NC_006840.2. DR RefSeq; YP_205778.1; NC_006840.2. DR ProteinModelPortal; Q5E256; -. DR STRING; 312309.VF_2395; -. DR EnsemblBacteria; AAW86890; AAW86890; VF_2395. DR GeneID; 3279545; -. DR KEGG; vfi:VF_2395; -. DR PATRIC; 20115542; VBIVibFis127983_2430. DR eggNOG; ENOG4105C12; Bacteria. DR eggNOG; COG0151; LUCA. DR HOGENOM; HOG000033463; -. DR KO; K01945; -. DR OMA; VNGMAAE; -. DR OrthoDB; POG091H02DZ; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR HAMAP; MF_00138; GARS; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00138}; KW Complete proteome {ECO:0000313|Proteomes:UP000000537}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:AAW86890.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00138}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00138}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00138}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00138}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}; KW Reference proteome {ECO:0000313|Proteomes:UP000000537}. FT DOMAIN 109 316 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT METAL 286 286 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_00138}. FT METAL 288 288 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_00138}. SQ SEQUENCE 430 AA; 45730 MW; 1AE178734F1D0D67 CRC64; MNVLIIGAGG REHALGWKAA QNPNVETVFI APGNAGTALE PKLENVAIDV EDIAALVAFA KEKAIELTIV GPEAPLVIGV VDAFREADLP IFGPTKAAAQ LEGSKAFTKD FLARHDIPTG SYANFTEIEP ALAYVREQGA PIVVKADGLA AGKGVIVAMT LEEAEDAIKD MLAGNAFGEA GSRVVIEEFL EGEEASFIVM VDGASVLPMA TSQDHKRVGD KDTGPNTGGM GAYSPAPVVT PEIHNRILEE VIYPTVRGMD AEGAPYTGFL YAGLMIDTEG TPKVIEYNCR FGDPETQPIM MRMESDLVEL CLMAIDEKLD EAESKWDPRA SIGVVLAAGG YPADYAKGDV ISLPSEETEG QKIFHAGTTN NDAGDVVTNG GRVLCATALG NTVSEAQERA YELAKQVSWN GMFHRNDIGY RAIARELETK //