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 16-JAN-2019, entry version 104.
DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3;
DE Includes:
DE RecName: Full=Phosphoribosylamine--glycine ligase;
DE EC=6.3.4.13;
DE AltName: Full=Glycinamide ribonucleotide synthetase;
DE Short=GARS;
DE AltName: Full=Phosphoribosylglycinamide synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE EC=6.3.3.1;
DE AltName: Full=AIR synthase;
DE Short=AIRS;
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylglycinamide formyltransferase;
DE EC=2.1.2.2;
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;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(formamido)-N(1)-(5-phospho-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:58478,
CC ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) +
CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:57454, ChEBI:CHEBI:58426, ChEBI:CHEBI:58457;
CC EC=2.1.2.2;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC ribose 1-diphosphate: step 2/2.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
CC phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
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
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family.
CC {ECO:0000305}.
DR EMBL; AJ780930; CAG47113.1; -; Genomic_DNA.
DR EMBL; BC122573; AAI22574.1; -; mRNA.
DR RefSeq; NP_001035563.1; NM_001040473.2.
DR UniGene; Bt.11270; -.
DR UniGene; Bt.94801; -.
DR ProteinModelPortal; 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 VGNC; VGNC:29255; GART.
DR eggNOG; KOG0237; Eukaryota.
DR eggNOG; KOG3076; Eukaryota.
DR eggNOG; COG0150; LUCA.
DR eggNOG; COG0151; LUCA.
DR eggNOG; COG0299; LUCA.
DR GeneTree; ENSGT00390000000292; -.
DR HOGENOM; HOG000030315; -.
DR HOVERGEN; HBG008333; -.
DR InParanoid; Q59A32; -.
DR KO; K11787; -.
DR OMA; LLERHNC; -.
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 10 organ(s), highest expression level in heart.
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:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
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; Complete proteome; Ligase; Manganese;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Purine biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P22102}.
FT CHAIN 2 1010 Trifunctional purine biosynthetic protein
FT adenosine-3.
FT /FTId=PRO_0000250715.
FT DOMAIN 111 318 ATP-grasp.
FT NP_BIND 137 199 ATP. {ECO:0000250}.
FT REGION 434 809 AIRS.
FT REGION 810 1010 GART.
FT REGION 818 820 5'-phosphoribosylglycinamide binding.
FT {ECO:0000250}.
FT REGION 896 899 10-formyltetrahydrofolate binding.
FT {ECO:0000250}.
FT REGION 947 951 10-formyltetrahydrofolate binding.
FT {ECO:0000250}.
FT REGION 977 980 5'-phosphoribosylglycinamide binding.
FT {ECO:0000250}.
FT ACT_SITE 915 915 Proton donor. {ECO:0000250}.
FT METAL 288 288 Manganese. {ECO:0000250}.
FT METAL 290 290 Manganese. {ECO:0000250}.
FT BINDING 871 871 10-formyltetrahydrofolate. {ECO:0000250}.
FT BINDING 913 913 10-formyltetrahydrofolate. {ECO:0000250}.
FT SITE 951 951 Raises pKa of active site His.
FT {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P22102}.
FT MOD_RES 350 350 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P22102}.
FT MOD_RES 440 440 Phosphoserine.
FT {ECO:0000250|UniProtKB:P22102}.
FT MOD_RES 682 682 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P22102}.
FT MOD_RES 802 802 Phosphoserine.
FT {ECO:0000250|UniProtKB:P22102}.
FT VARIANT 771 771 K -> E. {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
//
