ID Q3TH49_MOUSE Unreviewed; 433 AA.
AC Q3TH49;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255};
DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864};
GN Name=Gart {ECO:0000313|MGI:MGI:95654};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE40349.1};
RN [1] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [6] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000313|EMBL:BAE40349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE40349.1};
RC TISSUE=Liver {ECO:0000313|EMBL:BAE40349.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
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 -!- SIMILARITY: Belongs to the GARS family.
CC {ECO:0000256|ARBA:ARBA00038345}.
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DR EMBL; AK168445; BAE40349.1; -; mRNA.
DR AlphaFoldDB; Q3TH49; -.
DR SMR; Q3TH49; -.
DR PeptideAtlas; Q3TH49; -.
DR Antibodypedia; 1063; 250 antibodies from 31 providers.
DR UCSC; uc007zxw.1; mouse.
DR AGR; MGI:95654; -.
DR MGI; MGI:95654; Gart.
DR VEuPathDB; HostDB:ENSMUSG00000022962; -.
DR HOGENOM; CLU_027420_3_1_1; -.
DR OMA; EVMQACC; -.
DR UniPathway; UPA00074; UER00125.
DR ChiTaRS; Gart; mouse.
DR ExpressionAtlas; Q3TH49; baseline and differential.
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-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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; 45698 MW; C6B2789DB78932D7 CRC64;
MAARVLVIGS GGREHTLAWK LAQSPQVKQV LVAPGNAGTA CAGKISNAAV SVNDHSALAQ
FCKDEKIELV VVGPEAPLAA GIVGDLTSAG VRCFGPTAQA AQLESSKKFA KEFMDRHEIP
TAQWRAFTNP EDACSFITSA NFPALVVKAS GLAAGKGVIV AKSQAEACRA VQEIMQEKSF
GAAGETVVVE EFLEGEEVSC LCFTDGKTVA EMPPAQDHKR LLDGDEGPNT GGMGAYCPAP
QVSKDLLVKI KNTILQRAVD GMQQEGAPYT GILYAGIMLT KDGPKVLEFN CRFGDPECQV
ILPLLKSDLY EVMQSTLDGL LSASLPVWLE NHSAVTVVMA SKGYPGAYTK GVEITGFPEA
QALGLQVFHA GTALKDGKVV TSGGRVLTVT AVQENLMSAL AEARKGLAAL KFEGAIYRKD
IGFRAVAFLQ RPR
//