ID Q5E256_ALIF1 Unreviewed; 430 AA. AC Q5E256; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 12-OCT-2022, entry version 122. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255, 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 ORFNames=VF_2395 {ECO:0000313|EMBL:AAW86890.1}; OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC 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 with RT pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). 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:0000256|HAMAP-Rule:MF_00138}; 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:0000256|ARBA:ARBA00005174, CC ECO:0000256|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {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 STRING; 312309.VF_2395; -. DR EnsemblBacteria; AAW86890; AAW86890; VF_2395. DR KEGG; vfi:VF_2395; -. DR PATRIC; fig|312309.11.peg.2430; -. DR eggNOG; COG0151; Bacteria. DR HOGENOM; CLU_027420_3_1_6; -. DR OMA; KATVCKY; -. DR OrthoDB; 932854at2; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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; 3.30.1490.20; -; 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; 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 PANTHER; PTHR43472; PTHR43472; 1. 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|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00138}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_00138}; Reference proteome {ECO:0000313|Proteomes:UP000000537}. FT DOMAIN 109..316 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 212..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //