ID Q5PPK3_RAT Unreviewed; 433 AA. AC Q5PPK3; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255}; DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255}; GN Name=Gart {ECO:0000313|EMBL:AAH87644.1, ECO:0000313|RGD:1308717}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH87644.1}; RN [1] {ECO:0000313|EMBL:AAH87644.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain {ECO:0000313|EMBL:AAH87644.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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 --------------------------------------------------------------------------- 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; BC087644; AAH87644.1; -; mRNA. DR AlphaFoldDB; Q5PPK3; -. DR UCSC; RGD:1308717; rat. DR AGR; RGD:1308717; -. DR RGD; 1308717; Gart. DR PhylomeDB; Q5PPK3; -. DR UniPathway; UPA00074; UER00125. DR GO; GO:0005829; C:cytosol; ISO:RGD. 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; IDA:RGD. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IDA:RGD. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IDA:RGD. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; ISO:RGD. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:RGD. DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; ISO:RGD. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR GO; GO:0003360; P:brainstem development; IEP:RGD. DR GO; GO:0021549; P:cerebellum development; IEP:RGD. DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD. DR GO; GO:0006544; P:glycine metabolic process; IDA:RGD. DR GO; GO:0006177; P:GMP biosynthetic process; ISO:RGD. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0010035; P:response to inorganic substance; IDA:RGD. DR GO; GO:0010033; P:response to organic substance; IDA:RGD. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IDA:RGD. 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; IPR004733; PurM_cligase. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; TIGR00877; purD; 1. DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1. DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}. FT DOMAIN 111..318 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" SQ SEQUENCE 433 AA; 45711 MW; BB01FCA60E0BE3FB CRC64; MAARVLVIGS GGREHTLAWK LAQSPHVKQV LVAPGNAGTA SAGKISNAAV SINDHTALAR FCKDEKIELV VVGPEAPLAA GIVGDLTSAG VRCFGPTAQA ALLESSKKFA KEFMDRHGVP TAQWRAFTSP EDACSFIMSA DFPALVVKAS GLAAGKGVIV AKSKAEACEA VQEIMQEKSF GAAGETVVVE ELLEGEEVSC LCFTDGKTVA PMPPAQDHKR LLDGDRGPNT GGMGAYCPAP QVPKDLLVKI KNTILQRTVD GMQQEGVPYT GILYAGIMLT KDGPKVLEFN CRFGDPECQV ILPLLKSDLY EVIQSTFDGL LSESPPVWLE NHSAVTVVMA SGGYPGAYTK GVEITGFPEA QALGLQVFHA GTALKDAKVV TSGGRVLTVT AVRENLMSAL DEARKGLAAL KFEGAVYRKD IGFRAVAFLQ RPR //