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Q64737 (PUR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trifunctional purine biosynthetic protein adenosine-3

Including the following 3 domains:

  1. Phosphoribosylamine--glycine ligase
    EC=6.3.4.13
    Alternative name(s):
    Glycinamide ribonucleotide synthetase
    Short name=GARS
    Phosphoribosylglycinamide synthetase
  2. Phosphoribosylformylglycinamidine cyclo-ligase
    EC=6.3.3.1
    Alternative name(s):
    AIR synthase
    Short name=AIRS
    Phosphoribosyl-aminoimidazole synthetase
  3. Phosphoribosylglycinamide formyltransferase
    EC=2.1.2.2
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylase
    GAR transformylase
    Short name=GART
Gene names
Name:Gart
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1010 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. HAMAP-Rule MF_00138

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP-Rule MF_00138

10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide. HAMAP-Rule MF_00138

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. HAMAP-Rule MF_00138

Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.

Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.

Tissue specificity

Detected in liver, kidney and brain. Ref.2

Sequence similarities

In the N-terminal section; belongs to the GARS family.

In the central section; belongs to the AIR synthase family.

In the C-terminal section; belongs to the GART family.

Contains 1 ATP-grasp domain.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

brainstem development

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

glycine metabolic process

Inferred from electronic annotation. Source: Ensembl

purine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to inorganic substance

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from electronic annotation. Source: Ensembl

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: InterPro

phosphoribosylamine-glycine ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoribosylformylglycinamidine cyclo-ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoribosylglycinamide formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q64737-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q64737-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-1010: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10101009Trifunctional purine biosynthetic protein adenosine-3 HAMAP-Rule MF_00138
PRO_0000074938

Regions

Domain111 – 318208ATP-grasp
Nucleotide binding137 – 19963ATP By similarity
Region434 – 807374AIRS HAMAP-Rule MF_00138
Region808 – 1010203GART HAMAP-Rule MF_00138
Region818 – 82035'-phosphoribosylglycinamide binding By similarity
Region896 – 899410-formyltetrahydrofolate binding By similarity
Region947 – 951510-formyltetrahydrofolate binding By similarity
Region977 – 98045'-phosphoribosylglycinamide binding By similarity

Sites

Active site9151Proton donor By similarity
Metal binding2881Manganese By similarity
Metal binding2901Manganese By similarity
Binding site871110-formyltetrahydrofolate By similarity
Binding site913110-formyltetrahydrofolate By similarity
Site9511Raises pKa of active site His By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3501N6-acetyllysine By similarity

Natural variations

Alternative sequence434 – 1010577Missing in isoform Short.
VSP_005518

Experimental info

Sequence conflict411C → G in AAA19012. Ref.1
Sequence conflict411C → G in AAA19013. Ref.1
Sequence conflict411C → G in AAC53250. Ref.2
Sequence conflict411C → G in AAC53251. Ref.2
Sequence conflict3181D → G in AAC53250. Ref.2
Sequence conflict3181D → G in AAC53251. Ref.2
Sequence conflict5631G → A in AAA19013. Ref.1
Sequence conflict6901I → T in AAA19013. Ref.1
Sequence conflict8681Y → S in AAA19013. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 894D7D07D3C258B2

FASTA1,010107,503
        10         20         30         40         50         60 
MAARVLVIGS GGREHTLAWK LAQSPQVKQV LVAPGNAGTA CAGKISNAAV SVNDHSALAQ 

        70         80         90        100        110        120 
FCKDEKIELV VVGPEAPLAA GIVGDLTSAG VRCFGPTAQA AQLESSKKFA KEFMDRHEIP 

       130        140        150        160        170        180 
TAQWRAFTNP EDACSFITSA NFPALVVKAS GLAAGKGVIV AKSQAEACRA VQEIMQEKSF 

       190        200        210        220        230        240 
GAAGETVVVE EFLEGEEVSC LCFTDGKTVA EMPPAQDHKR LLDGDEGPNT GGMGAYCPAP 

       250        260        270        280        290        300 
QVSKDLLVKI KNTILQRAVD GMQQEGAPYT GILYAGIMLT KDGPKVLEFN CRFGDPECQV 

       310        320        330        340        350        360 
ILPLLKSDLY EVMQSTLDGL LSASLPVWLE NHSAVTVVMA SKGYPGAYTK GVEITGFPEA 

       370        380        390        400        410        420 
QALGLQVFHA GTALKDGKVV TSGGRVLTVT AVQENLMSAL AEARKGLAAL KFEGAIYRKD 

       430        440        450        460        470        480 
IGFRAVAFLQ RPRGLTYKDS GVDIAAGNML VKKIQPLAKA TSRPGCSVDL GGFAGLFDLK 

       490        500        510        520        530        540 
AAGFKDPLLA SGTDGVGTKL KIAQLCNKHD SIGQDLVAMC VNDILAQGAE PLFFLDYFSC 

       550        560        570        580        590        600 
GKLDLSTTEA VIAGIAAACQ QAGCALLGGE TAEMPNMYPP GEYDLAGFAV GAMERHQKLP 

       610        620        630        640        650        660 
QLERITEGDA VIGVASSGLH SNGFSLVRKI VERSSLQYSS PAPGGCGDQT LGDLLLTPTR 

       670        680        690        700        710        720 
IYSHSLLPII RSGRVKAFAH ITGGGLLENI PRVLPQKFGV DLDASTWRVP KVFSWLQQEG 

       730        740        750        760        770        780 
ELSEEEMART FNCGIGAALV VSKDQAEQVL HDVRRRQEEA WVIGSVVACP EDSPRVRVKN 

       790        800        810        820        830        840 
LIETIQTNGS LVANGFLKSN FPVQQKKARV AVLISGTGSN LQALIDSTRD PKSSSHIVLV 

       850        860        870        880        890        900 
ISNKAAVAGL DRAERAGIPT RVINHKLYKN RVEFDNAVDH VLEEFSVDIV CLAGFMRILS 

       910        920        930        940        950        960 
GPFVRKWDGK MLNIHPSLLP SFKGSNAHEQ VLEAGVTITG CTVHFVAEDV DAGQIILQEA 

       970        980        990       1000       1010 
VPVRRGDTVA TLSERVKVAE HKIFPAALQL VASGAVQLRE DGKIHWAKEQ 

« Hide

Isoform Short [UniParc].

Checksum: C6B2789DB78932D7
Show »

FASTA43345,698

References

« Hide 'large scale' references
[1]"Mouse cDNAs encoding a trifunctional protein of de novo purine synthesis and a related single-domain glycinamide ribonucleotide synthetase."
Kan J.L., Jannatipour M., Taylor S.M., Moran R.G.
Gene 137:195-202(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Strain: C57BL/6 X CBA.
Tissue: Spleen.
[2]"Analysis of a mouse gene encoding three steps of purine synthesis reveals use of an intronic polyadenylation signal without alternative exon usage."
Kan J.L., Moran R.G.
J. Biol. Chem. 270:1823-1832(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney, Liver and Stomach.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Strain: C57BL/6.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01023 mRNA. Translation: AAA19012.1.
U01024 mRNA. Translation: AAA19013.1.
U20886 expand/collapse EMBL AC list , U20875, U20876, U20877, U20879, U20880, U20881, U20882, U20883 Genomic DNA. Translation: AAC53250.1.
U20892 expand/collapse EMBL AC list , U20875, U20876, U20877, U20879, U20880, U20881, U20882, U20883, U20886, U20884, U20887, U20885, U20889, U20890, U20891 Genomic DNA. Translation: AAC53251.1.
AK168501 mRNA. Translation: BAE40386.1.
AK168724 mRNA. Translation: BAE40565.1.
AK168796 mRNA. Translation: BAE40629.1.
AK168864 mRNA. Translation: BAE40683.1.
AK168876 mRNA. Translation: BAE40694.1.
CH466602 Genomic DNA. Translation: EDL03819.1.
BC070465 mRNA. Translation: AAH70465.1.
CCDSCCDS28329.1. [Q64737-1]
PIRI67805.
RefSeqNP_034386.2. NM_010256.2. [Q64737-1]
XP_006522973.1. XM_006522910.1. [Q64737-1]
XP_006522974.1. XM_006522911.1. [Q64737-1]
XP_006522975.1. XM_006522912.1. [Q64737-1]
UniGeneMm.4505.

3D structure databases

ProteinModelPortalQ64737.
SMRQ64737. Positions 1-430, 475-785, 808-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199831. 1 interaction.
IntActQ64737. 1 interaction.
MINTMINT-1852011.

Chemistry

BindingDBQ64737.
ChEMBLCHEMBL3690.
GuidetoPHARMACOLOGY2612.

PTM databases

PhosphoSiteQ64737.

Proteomic databases

MaxQBQ64737.
PaxDbQ64737.
PRIDEQ64737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023684; ENSMUSP00000023684; ENSMUSG00000022962. [Q64737-1]
ENSMUST00000120450; ENSMUSP00000114034; ENSMUSG00000022962. [Q64737-2]
GeneID14450.
KEGGmmu:14450.
UCSCuc007zxu.1. mouse. [Q64737-1]

Organism-specific databases

CTD2618.
MGIMGI:95654. Gart.

Phylogenomic databases

eggNOGCOG0151.
GeneTreeENSGT00390000000292.
HOGENOMHOG000030315.
HOVERGENHBG008333.
InParanoidQ3TGI3.
KOK11787.
OMATARYESF.
OrthoDBEOG7RBZ7H.
TreeFamTF106368.

Enzyme and pathway databases

SABIO-RKQ64737.
UniPathwayUPA00074; UER00125.
UPA00074; UER00126.
UPA00074; UER00129.

Gene expression databases

ArrayExpressQ64737.
BgeeQ64737.
CleanExMM_GART.
GenevestigatorQ64737.

Family and domain databases

Gene3D3.30.1330.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.170. 1 hit.
3.40.50.20. 1 hit.
3.90.600.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPMF_00138. GARS.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR016185. PreATP-grasp_dom.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
IPR000115. PRibGlycinamide_synth.
IPR020560. PRibGlycinamide_synth_C-dom.
IPR020559. PRibGlycinamide_synth_CS.
IPR020562. PRibGlycinamide_synth_N.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
IPR004607. PurN_trans.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
PF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF53328. SSF53328. 1 hit.
SSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsTIGR00877. purD. 1 hit.
TIGR00878. purM. 1 hit.
TIGR00639. PurN. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGART. mouse.
NextBio286065.
PROQ64737.
SOURCESearch...

Entry information

Entry namePUR2_MOUSE
AccessionPrimary (citable) accession number: Q64737
Secondary accession number(s): Q3TGI3, Q6NS48
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot