GenomeNet

Database: UniProt
Entry: Q59A32
LinkDB: Q59A32
Original site: Q59A32 
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
//
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