PUR2_BOVIN
ID PUR2_BOVIN Reviewed; 1010 AA.
AC Q59A32;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-771.
RX PubMed=15777723; DOI=10.1016/j.gene.2004.12.038;
RA Woehlke A., Droegemueller C., Kuiper H., Leeb T., Distl O.;
RT "Molecular characterization and chromosomal assignment of the bovine
RT glycinamide ribonucleotide formyltransferase (GART) gene on cattle
RT chromosome 1q12.1-q12.2.";
RL Gene 348:73-81(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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; AJ780930; CAG47113.1; -; Genomic_DNA.
DR EMBL; BC122573; AAI22574.1; -; mRNA.
DR RefSeq; NP_001035563.1; NM_001040473.2.
DR AlphaFoldDB; Q59A32; -.
DR SMR; Q59A32; -.
DR STRING; 9913.ENSBTAP00000012108; -.
DR PaxDb; Q59A32; -.
DR PeptideAtlas; Q59A32; -.
DR PRIDE; Q59A32; -.
DR Ensembl; ENSBTAT00000012108; ENSBTAP00000012108; ENSBTAG00000009188.
DR GeneID; 281183; -.
DR KEGG; bta:281183; -.
DR CTD; 2618; -.
DR VEuPathDB; HostDB:ENSBTAG00000009188; -.
DR VGNC; VGNC:29255; GART.
DR eggNOG; KOG0237; Eukaryota.
DR eggNOG; KOG3076; Eukaryota.
DR GeneTree; ENSGT00390000000292; -.
DR HOGENOM; CLU_005361_0_2_1; -.
DR InParanoid; Q59A32; -.
DR OMA; EVMQACC; -.
DR OrthoDB; 105366at2759; -.
DR TreeFam; TF106368; -.
DR Reactome; R-BTA-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00125.
DR UniPathway; UPA00074; UER00126.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000009188; Expressed in conceptus and 107 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW 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_0000250715"
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 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT VARIANT 771
FT /note="K -> E"
FT /evidence="ECO:0000269|PubMed:15777723"
SQ SEQUENCE 1010 AA; 107907 MW; 27DFCA438661A771 CRC64;
MAARVLVIGN GGREHTLAWK LAQSTHVKQV LVTPGNAGTA CSEKISNTDI SISDHTALAQ
FCKDEKIEFV VVGPEAPLAA GIVGNLNSVG VRCFGPTAQA AQLESSKRFA KEFMDRHGIS
TARWRAFTKP KEACDFIMSA DFPALVVKAS GLAAGKGVIV AKSKEEACEA VREIMQGKAF
GEAGETVVIE ELLEGEEVSC LCFTDGRTVA PMPPAQDHKR LLEGDEGPNT GGMGAYCPAP
QVSKDLLLKI KNNILQRTVD GMQEEGMPYT GVLYAGIMLT KNGPKVLEFN CRFGDPECQV
ILPLLKSDLY EVIQSILDGL LCTSLPVWLD NCAAVTVVMA SKGYPGDYTK GVEITGFPEA
QALGLEVFQA GTALKDGKVV TNGGRVLTVT AIRENLISAL EEARKGLAAI KFEGAVYRKD
IGFRAIAFLQ QPRGLTYKES GVDIAAGNML VQKIKPLAKA TSRPGCDVDL GGFAGLFDLK
AAGFTDPLLA CGTDGVGTKL KIAQQCSKHD TIGQDLVAMC VNDILAQGAE PLFFLDYFSC
GKLDLRTTEA VITGIAKACK KAGCALLGGE TAEMPDMYPP GEYDLAGFAV GAMERDQKLP
QLERITEGDA VIGIASSGLH SNGFSLVRKI VAKSSLEYSS PAPGGCGDQT LGDLLLTPTK
IYSRSLLPVL RSGRVKAVAH ITGGGLLENI PRVLPQKLGV NLDAQTWRVP RIFSWLQQEG
HLSEEEMART FNCGIGAALV VSEDLVKQTL QDIEQHQEEA CVIGRVVACP KGSPRVKVEH
LIETMQINGS VLENGTLRNH FSVQPKKARV AVLISGTGSN LQALIDSTRE PSSLAHIVIV
ISNKAAVAGL DKAEKAGIPT RVINHKLYKN RAAFDTAIDE VLEEFSTDIV CLAGFMRILS
GPFVRKWNGK MLNIHPSLLP SFKGSNAHEQ VLDAGVTVTG CTVHFVAEDV DAGQIILQEA
VPVKRGDTVE TLSERVKLAE HKIFPSALQL VASGAVRLGE NGRICWVTED
