Trifunctional purine biosynthetic protein adenosine-3

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Q59A32 (PUR2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 65. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Trifunctional purine biosynthetic protein adenosine-3

Including the following 3 domains:

Phosphoribosylamine--glycine ligase
EC=6.3.4.13
Alternative name(s):
Glycinamide ribonucleotide synthetase
Short name=GARS
Phosphoribosylglycinamide synthetase
Phosphoribosylformylglycinamidine cyclo-ligase
EC=6.3.3.1
Alternative name(s):
AIR synthase
Short name=AIRS
Phosphoribosyl-aminoimidazole synthetase
Phosphoribosylglycinamide formyltransferase
EC=2.1.2.2
Alternative name(s):
5'-phosphoribosylglycinamide transformylase
GAR transformylase
Short name=GART

Gene names

Name:

GART

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1010 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity

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

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

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

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.

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.

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 process	Purine biosynthesis
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase Transferase
PTM	Acetylation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway methylation Inferred from electronic annotation. Source: GOC purine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP 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: EC phosphoribosylformylglycinamidine cyclo-ligase activity Inferred from electronic annotation. Source: EC phosphoribosylglycinamide formyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1010

1010

Trifunctional purine biosynthetic protein adenosine-3

PRO_0000250715

Regions

Domain

111 – 318

208

ATP-grasp

Nucleotide binding

137 – 199

ATP By similarity

Region

434 – 809

376

AIRS

Region

810 – 1010

201

GART

Region

818 – 820

5'-phosphoribosylglycinamide binding By similarity

Region

896 – 899

10-formyltetrahydrofolate binding By similarity

Region

947 – 951

10-formyltetrahydrofolate binding By similarity

Region

977 – 980

5'-phosphoribosylglycinamide binding By similarity

Sites

Active site

915

Proton donor By similarity

Metal binding

288

Manganese By similarity

Metal binding

290

Manganese By similarity

Binding site

871

10-formyltetrahydrofolate By similarity

Binding site

913

10-formyltetrahydrofolate By similarity

Site

951

Raises pKa of active site His By similarity

Amino acid modifications

Modified residue

350

N6-acetyllysine By similarity

Natural variations

Natural variant

771

K → E. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q59A32 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 27DFCA438661A771
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FASTA

1,010

107,907

        10         20         30         40         50         60 
MAARVLVIGN GGREHTLAWK LAQSTHVKQV LVTPGNAGTA CSEKISNTDI SISDHTALAQ 

        70         80         90        100        110        120 
FCKDEKIEFV VVGPEAPLAA GIVGNLNSVG VRCFGPTAQA AQLESSKRFA KEFMDRHGIS 

       130        140        150        160        170        180 
TARWRAFTKP KEACDFIMSA DFPALVVKAS GLAAGKGVIV AKSKEEACEA VREIMQGKAF 

       190        200        210        220        230        240 
GEAGETVVIE ELLEGEEVSC LCFTDGRTVA PMPPAQDHKR LLEGDEGPNT GGMGAYCPAP 

       250        260        270        280        290        300 
QVSKDLLLKI KNNILQRTVD GMQEEGMPYT GVLYAGIMLT KNGPKVLEFN CRFGDPECQV 

       310        320        330        340        350        360 
ILPLLKSDLY EVIQSILDGL LCTSLPVWLD NCAAVTVVMA SKGYPGDYTK GVEITGFPEA 

       370        380        390        400        410        420 
QALGLEVFQA GTALKDGKVV TNGGRVLTVT AIRENLISAL EEARKGLAAI KFEGAVYRKD 

       430        440        450        460        470        480 
IGFRAIAFLQ QPRGLTYKES GVDIAAGNML VQKIKPLAKA TSRPGCDVDL GGFAGLFDLK 

       490        500        510        520        530        540 
AAGFTDPLLA CGTDGVGTKL KIAQQCSKHD TIGQDLVAMC VNDILAQGAE PLFFLDYFSC 

       550        560        570        580        590        600 
GKLDLRTTEA VITGIAKACK KAGCALLGGE TAEMPDMYPP GEYDLAGFAV GAMERDQKLP 

       610        620        630        640        650        660 
QLERITEGDA VIGIASSGLH SNGFSLVRKI VAKSSLEYSS PAPGGCGDQT LGDLLLTPTK 

       670        680        690        700        710        720 
IYSRSLLPVL RSGRVKAVAH ITGGGLLENI PRVLPQKLGV NLDAQTWRVP RIFSWLQQEG 

       730        740        750        760        770        780 
HLSEEEMART FNCGIGAALV VSEDLVKQTL QDIEQHQEEA CVIGRVVACP KGSPRVKVEH 

       790        800        810        820        830        840 
LIETMQINGS VLENGTLRNH FSVQPKKARV AVLISGTGSN LQALIDSTRE PSSLAHIVIV 

       850        860        870        880        890        900 
ISNKAAVAGL DKAEKAGIPT RVINHKLYKN RAAFDTAIDE VLEEFSTDIV CLAGFMRILS 

       910        920        930        940        950        960 
GPFVRKWNGK MLNIHPSLLP SFKGSNAHEQ VLDAGVTVTG CTVHFVAEDV DAGQIILQEA 

       970        980        990       1000       1010 
VPVKRGDTVE TLSERVKLAE HKIFPSALQL VASGAVRLGE NGRICWVTED

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization and chromosomal assignment of the bovine glycinamide ribonucleotide formyltransferase (GART) gene on cattle chromosome 1q12.1-q12.2." Woehlke A., Droegemueller C., Kuiper H., Leeb T., Distl O. Gene 348:73-81(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-771.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ780930 Genomic DNA. Translation: CAG47113.1. BC122573 mRNA. Translation: AAI22574.1.
IPI	IPI00709162.
RefSeq	NP_001035563.1. NM_001040473.2.
UniGene	Bt.11270. Bt.94801.
3D structure databases
HSSP	HSSP built from PDB template 1ZLY based on UniProtKB P22102.
ProteinModelPortal	Q59A32.
SMR	Q59A32. Positions 1-430, 475-792, 808-1007.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000012108.
Proteomic databases
PaxDb	Q59A32.
PRIDE	Q59A32.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000012108; ENSBTAP00000012108; ENSBTAG00000009188.
GeneID	281183.
KEGG	bta:281183.
Organism-specific databases
CTD	2618.
Phylogenomic databases
eggNOG	COG0151.
GeneTree	ENSGT00390000000292.
HOGENOM	HOG000030315.
HOVERGEN	HBG008333.
InParanoid	Q59A32.
KO	K11787.
OMA	GETSEMP.
OrthoDB	EOG4FFD13.
Enzyme and pathway databases
UniPathway	UPA00074; UER00125. UPA00074; UER00126. UPA00074; UER00129.
Gene expression databases
ArrayExpress	Q59A32.
Family and domain databases
Gene3D	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.
InterPro	IPR010918. 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]
Pfam	PF00586. 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]
SUPFAM	SSF56042. AIR_synth_C. 1 hit. SSF53328. formyl_transf. 1 hit. SSF52440. PreATP-grasp-like. 1 hit. SSF55326. PurM_N-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
TIGRFAMs	TIGR00877. purD. 1 hit. TIGR00878. purM. 1 hit. TIGR00639. PurN. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00184. GARS. 1 hit. PS00373. GART. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20805240.

Entry information

Entry name

PUR2_BOVIN

Accession

Primary (citable) accession number: Q59A32

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	April 26, 2005
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents