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   27-MAR-2024, entry version 191.
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,
RC   Pancreas, 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=(6R)-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:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
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, ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         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.
DR   RefSeq; XP_006522975.1; XM_006522912.1.
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   GlyGen; Q64737; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q64737; -.
DR   MetOSite; Q64737; -.
DR   PhosphoSitePlus; Q64737; -.
DR   SwissPalm; Q64737; -.
DR   EPD; Q64737; -.
DR   jPOST; Q64737; -.
DR   MaxQB; Q64737; -.
DR   PaxDb; 10090-ENSMUSP00000023684; -.
DR   PeptideAtlas; Q64737; -.
DR   ProteomicsDB; 302030; -. [Q64737-1]
DR   ProteomicsDB; 302031; -. [Q64737-2]
DR   Pumba; Q64737; -.
DR   Antibodypedia; 1063; 250 antibodies from 31 providers.
DR   DNASU; 14450; -.
DR   Ensembl; ENSMUST00000023684.14; ENSMUSP00000023684.8; ENSMUSG00000022962.16. [Q64737-1]
DR   Ensembl; ENSMUST00000120450.2; ENSMUSP00000114034.2; ENSMUSG00000022962.16. [Q64737-2]
DR   Ensembl; ENSMUST00000231380.2; ENSMUSP00000156232.2; ENSMUSG00000022962.16. [Q64737-2]
DR   Ensembl; ENSMUST00000232289.2; ENSMUSP00000156002.2; ENSMUSG00000022962.16. [Q64737-1]
DR   GeneID; 14450; -.
DR   KEGG; mmu:14450; -.
DR   UCSC; uc007zxu.1; mouse. [Q64737-1]
DR   AGR; MGI:95654; -.
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; 729at2759; -.
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 78 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 292 other cell types or tissues.
DR   ExpressionAtlas; Q64737; baseline and differential.
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:0046654; P:tetrahydrofolate biosynthetic process; ISO:MGI.
DR   CDD; cd08645; FMT_core_GART; 1.
DR   CDD; cd02196; PurM; 1.
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; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   NCBIfam; TIGR00877; purD; 1.
DR   NCBIfam; TIGR00878; purM; 1.
DR   NCBIfam; TIGR00639; PurN; 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; 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; SM01209; GARS_A; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
DR   PROSITE; PS00373; GART; 1.
DR   Genevisible; Q64737; MM.
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="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         896..899
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         913
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         947..951
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
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
//