PUR2_MOUSE
ID PUR2_MOUSE Reviewed; 1010 AA.
AC Q64737; Q3TGI3; Q6NS48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000250|UniProtKB:P22102};
DE Includes:
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000250|UniProtKB:P22102};
DE EC=6.3.4.13 {ECO:0000250|UniProtKB:P22102};
DE AltName: Full=Glycinamide ribonucleotide synthetase;
DE Short=GARS;
DE AltName: Full=Phosphoribosylglycinamide synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000250|UniProtKB:P22102};
DE EC=6.3.3.1 {ECO:0000250|UniProtKB:P22102};
DE AltName: Full=AIR synthase;
DE Short=AIRS;
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000250|UniProtKB:P22102};
DE EC=2.1.2.2 {ECO:0000250|UniProtKB:P22102};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase;
DE AltName: Full=GAR transformylase;
DE Short=GART;
GN Name=Gart;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=C57BL/6 X CBA; TISSUE=Spleen;
RX PubMed=8299947; DOI=10.1016/0378-1119(93)90006-o;
RA Kan J.L., Jannatipour M., Taylor S.M., Moran R.G.;
RT "Mouse cDNAs encoding a trifunctional protein of de novo purine synthesis
RT and a related single-domain glycinamide ribonucleotide synthetase.";
RL Gene 137:195-202(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=7829519; DOI=10.1074/jbc.270.4.1823;
RA Kan J.L., Moran R.G.;
RT "Analysis of a mouse gene encoding three steps of purine synthesis reveals
RT use of an intronic polyadenylation signal without alternative exon usage.";
RL J. Biol. Chem. 270:1823-1832(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Liver, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Trifunctional enzyme that catalyzes three distinct reactions
CC as part of the 'de novo' inosine monophosphate biosynthetic pathway.
CC {ECO:0000250|UniProtKB:P22102}.
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:0000250|UniProtKB:P22102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17454;
CC Evidence={ECO:0000250|UniProtKB:P22102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000250|UniProtKB:P22102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23033;
CC Evidence={ECO:0000250|UniProtKB:P22102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
CC EC=2.1.2.2; Evidence={ECO:0000250|UniProtKB:P22102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15054;
CC Evidence={ECO:0000250|UniProtKB:P22102};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P15640,
CC ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 1 magnesium or manganese ion per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2.
CC {ECO:0000250|UniProtKB:P22102}.
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:0000250|UniProtKB:P22102}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC {ECO:0000250|UniProtKB:P22102}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22102}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q64737-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q64737-2; Sequence=VSP_005518;
CC -!- TISSUE SPECIFICITY: Detected in liver, kidney and brain.
CC {ECO:0000269|PubMed:7829519}.
CC -!- DOMAIN: The N-terminal ATP-grasp domain carries the
CC phosphoribosylamine--glycine ligase activity.
CC {ECO:0000250|UniProtKB:P22102}.
CC -!- DOMAIN: The central AIRS domain carries the
CC phosphoribosylformylglycinamidine cyclo-ligase activity.
CC {ECO:0000250|UniProtKB:P22102}.
CC -!- DOMAIN: The C-terminal GART domain carries the
CC phosphoribosylglycinamide formyltransferase activity.
CC {ECO:0000250|UniProtKB:P22102}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the AIR synthase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family.
CC {ECO:0000305}.
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DR EMBL; U01023; AAA19012.1; -; mRNA.
DR EMBL; U01024; AAA19013.1; -; mRNA.
DR EMBL; U20886; AAC53250.1; -; Genomic_DNA.
DR EMBL; U20875; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20876; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20877; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20879; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20880; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20881; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20882; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20883; AAC53250.1; JOINED; Genomic_DNA.
DR EMBL; U20892; AAC53251.1; -; Genomic_DNA.
DR EMBL; U20875; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20876; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20877; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20879; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20880; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20881; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20882; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20883; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20886; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20884; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20887; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20885; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20889; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20890; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; U20891; AAC53251.1; JOINED; Genomic_DNA.
DR EMBL; AK168501; BAE40386.1; -; mRNA.
DR EMBL; AK168724; BAE40565.1; -; mRNA.
DR EMBL; AK168796; BAE40629.1; -; mRNA.
DR EMBL; AK168864; BAE40683.1; -; mRNA.
DR EMBL; AK168876; BAE40694.1; -; mRNA.
DR EMBL; CH466602; EDL03819.1; -; Genomic_DNA.
DR EMBL; BC070465; AAH70465.1; -; mRNA.
DR CCDS; CCDS28329.1; -. [Q64737-1]
DR PIR; I67805; I67805.
DR RefSeq; NP_034386.2; NM_010256.2. [Q64737-1]
DR RefSeq; XP_006522973.1; XM_006522910.3.
DR RefSeq; XP_006522974.1; XM_006522911.2. [Q64737-1]
DR RefSeq; XP_006522975.1; XM_006522912.1. [Q64737-1]
DR AlphaFoldDB; Q64737; -.
DR SMR; Q64737; -.
DR BioGRID; 199831; 6.
DR STRING; 10090.ENSMUSP00000023684; -.
DR BindingDB; Q64737; -.
DR ChEMBL; CHEMBL3690; -.
DR DrugCentral; Q64737; -.
DR GuidetoPHARMACOLOGY; 2612; -.
DR iPTMnet; Q64737; -.
DR PhosphoSitePlus; Q64737; -.
DR SwissPalm; Q64737; -.
DR EPD; Q64737; -.
DR jPOST; Q64737; -.
DR MaxQB; Q64737; -.
DR PaxDb; Q64737; -.
DR PeptideAtlas; Q64737; -.
DR PRIDE; Q64737; -.
DR ProteomicsDB; 302030; -. [Q64737-1]
DR ProteomicsDB; 302031; -. [Q64737-2]
DR Antibodypedia; 1063; 214 antibodies from 31 providers.
DR DNASU; 14450; -.
DR Ensembl; ENSMUST00000023684; ENSMUSP00000023684; ENSMUSG00000022962. [Q64737-1]
DR Ensembl; ENSMUST00000120450; ENSMUSP00000114034; ENSMUSG00000022962. [Q64737-2]
DR Ensembl; ENSMUST00000231380; ENSMUSP00000156232; ENSMUSG00000022962. [Q64737-2]
DR Ensembl; ENSMUST00000232289; ENSMUSP00000156002; ENSMUSG00000022962. [Q64737-1]
DR GeneID; 14450; -.
DR KEGG; mmu:14450; -.
DR UCSC; uc007zxu.1; mouse. [Q64737-1]
DR CTD; 2618; -.
DR MGI; MGI:95654; Gart.
DR VEuPathDB; HostDB:ENSMUSG00000022962; -.
DR eggNOG; KOG0237; Eukaryota.
DR eggNOG; KOG3076; Eukaryota.
DR GeneTree; ENSGT00390000000292; -.
DR HOGENOM; CLU_005361_0_2_1; -.
DR InParanoid; Q64737; -.
DR OMA; EVMQACC; -.
DR OrthoDB; 105366at2759; -.
DR PhylomeDB; Q64737; -.
DR TreeFam; TF106368; -.
DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
DR SABIO-RK; Q64737; -.
DR UniPathway; UPA00074; UER00125.
DR UniPathway; UPA00074; UER00126.
DR UniPathway; UPA00074; UER00129.
DR BioGRID-ORCS; 14450; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Gart; mouse.
DR PRO; PR:Q64737; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q64737; protein.
DR Bgee; ENSMUSG00000022962; Expressed in ileal epithelium and 288 other tissues.
DR ExpressionAtlas; Q64737; baseline and differential.
DR Genevisible; Q64737; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; ISO:MGI.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; ISO:MGI.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:MGI.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:MGI.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IDA:MGI.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR GO; GO:0003360; P:brainstem development; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0006544; P:glycine metabolic process; ISO:MGI.
DR GO; GO:0006177; P:GMP biosynthetic process; IDA:MGI.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; ISO:MGI.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISO:MGI.
DR CDD; cd08645; FMT_core_GART; 1.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_00741; AIRS; 1.
DR HAMAP; MF_00138; GARS; 1.
DR HAMAP; MF_01930; PurN; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004607; GART.
DR InterPro; IPR001555; GART_AS.
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; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 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 SUPFAM; SSF53328; SSF53328; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
DR TIGRFAMs; TIGR00639; PurN; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS00373; GART; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Ligase; Magnesium;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Purine biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT CHAIN 2..1010
FT /note="Trifunctional purine biosynthetic protein adenosine-
FT 3"
FT /id="PRO_0000074938"
FT DOMAIN 111..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 434..809
FT /note="AIRS domain"
FT /evidence="ECO:0000250|UniProtKB:P21872"
FT REGION 810..1010
FT /note="GART domain"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT ACT_SITE 915
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08179"
FT BINDING 190..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 818..820
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 871
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 896..899
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 913
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 947..951
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 977..980
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT SITE 951
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000250|UniProtKB:P08179"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT VAR_SEQ 434..1010
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8299947"
FT /id="VSP_005518"
FT CONFLICT 41
FT /note="C -> G (in Ref. 1; AAA19012/AAA19013 and 2;
FT AAC53250/AAC53251)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="D -> G (in Ref. 2; AAC53250/AAC53251)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="G -> A (in Ref. 1; AAA19013)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="I -> T (in Ref. 1; AAA19013)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="Y -> S (in Ref. 1; AAA19013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1010 AA; 107503 MW; 894D7D07D3C258B2 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 RPRGLTYKDS GVDIAAGNML VKKIQPLAKA TSRPGCSVDL GGFAGLFDLK
AAGFKDPLLA SGTDGVGTKL KIAQLCNKHD SIGQDLVAMC VNDILAQGAE PLFFLDYFSC
GKLDLSTTEA VIAGIAAACQ QAGCALLGGE TAEMPNMYPP GEYDLAGFAV GAMERHQKLP
QLERITEGDA VIGVASSGLH SNGFSLVRKI VERSSLQYSS PAPGGCGDQT LGDLLLTPTR
IYSHSLLPII RSGRVKAFAH ITGGGLLENI PRVLPQKFGV DLDASTWRVP KVFSWLQQEG
ELSEEEMART FNCGIGAALV VSKDQAEQVL HDVRRRQEEA WVIGSVVACP EDSPRVRVKN
LIETIQTNGS LVANGFLKSN FPVQQKKARV AVLISGTGSN LQALIDSTRD PKSSSHIVLV
ISNKAAVAGL DRAERAGIPT RVINHKLYKN RVEFDNAVDH VLEEFSVDIV CLAGFMRILS
GPFVRKWDGK MLNIHPSLLP SFKGSNAHEQ VLEAGVTITG CTVHFVAEDV DAGQIILQEA
VPVRRGDTVA TLSERVKVAE HKIFPAALQL VASGAVQLRE DGKIHWAKEQ
