SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q26255

- PUR2_CHITE

UniProt

Q26255 - PUR2_CHITE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Trifunctional purine biosynthetic protein adenosine-3

Gene
GART
Organism
Chironomus tentans (Midge) (Camptochironomus tentans)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.UniRule annotation
10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi291 – 2911Manganese By similarity
Metal bindingi293 – 2931Manganese By similarity
Binding sitei1235 – 1235110-formyltetrahydrofolate By similarity
Binding sitei1277 – 1277110-formyltetrahydrofolate By similarity
Active sitei1279 – 12791Proton donor By similarity
Sitei1315 – 13151Raises pKa of active site His By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi141 – 20262ATP By similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methyltransferase activity Source: InterPro
  4. phosphoribosylamine-glycine ligase activity Source: UniProtKB-EC
  5. phosphoribosylformylglycinamidine cyclo-ligase activity Source: UniProtKB-EC
  6. phosphoribosylglycinamide formyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. purine nucleobase biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00125.
UPA00074; UER00126.
UPA00074; UER00129.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GART
OrganismiChironomus tentans (Midge) (Camptochironomus tentans)
Taxonomic identifieri7153 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraChironomoideaChironomidaeChironominaeChironomus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13711371Trifunctional purine biosynthetic protein adenosine-3UniRule annotationPRO_0000074933Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ26255.
SMRiQ26255. Positions 494-792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 321207ATP-graspAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni434 – 1171738AIRSUniRule annotationAdd
BLAST
Regioni1172 – 1371200GARTUniRule annotationAdd
BLAST
Regioni1180 – 118235'-phosphoribosylglycinamide binding By similarity
Regioni1260 – 1263410-formyltetrahydrofolate binding By similarity
Regioni1311 – 1315510-formyltetrahydrofolate binding By similarity
Regioni1341 – 134445'-phosphoribosylglycinamide binding By similarity

Sequence similaritiesi

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.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
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. 2 hits.
HAMAPiMF_00138. GARS.
InterProiIPR010918. 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]
PfamiPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
PF00551. Formyl_trans_N. 1 hit.
PF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF53328. SSF53328. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR00877. purD. 1 hit.
TIGR00878. purM. 2 hits.
TIGR00639. PurN. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q26255-1 [UniParc]FASTAAdd to Basket

« Hide

MTGKKLLLIG SGGREHALAW KLQQSKNVTE IFAFPGSIGI SQLEKVQLVN     50
NNEMNLKDFK GIASWCKINH IDLVIVGPED PLAEGIADQL KAANIHCFGP 100
SKAGARIESD KSWSKDFMIR HHIPTAQYGS FIDALKAKDF IRNTPNALVV 150
KASGLAAGKG VIVAENIEEA CAAVDEILGD HKFGTAGDVV VVEEKLSGQE 200
VSVLGFVDSN SVRILPPAQD HKRLKDNDEG LNTGGMGAYC PCPLISQQEL 250
DIVKSQVLQR AVDGLRKENI LYNGILYAGI MLTHDGPKTL EFNCRFGDPE 300
TQIILPLLDE DLYDLMMASC TNHLCNVPEL KFKSNINAVG VVMASKGYPE 350
TSTKGCVISG IESVETMDNH IVFHSGTSKN NKDEWITNGG RVLINIALAD 400
NLKKAADLAT KACDVVKFDG SQYRRDIGKK AFQIHSLTYK ESGVNIEAGN 450
SLVGRIKSLS YGTHRSGVVG QIGSFGGLMR LNDIKYINSN GEESNYKDIV 500
LVQGTDGVGT KLKIAESMNV WDTIGIDLVA MCVNDVLCNG AEPIGFLDYI 550
ACGHLEVPTV ATIVKGIADG CRKANCALIG GETAEMPSMY GKGKYDLAGY 600
CVGITEYDEI LPKINDVHVG DVVIGLPSSG IHSNGFSLVN KIFQQTGFKL 650
TDIAEFSDSH KSYGMEFLTP TRLYVSETLP FLRNGYVKAL AHITGGGLLE 700
NIPRILPNHL SVQIDALTWK LPKVFSWLAA HGNVNANEML RTFNCGIGMI 750
IIMPRNDIEW ETIPEARMIG SITQRDHNGP QVIVKNFKEV LHKEVTHWKK 800
GDAETTSISY KDSGVDITAG NELVDNIKPH AKSTNRKGVI GGLGSFGGLF 850
RINECGTKFE DPMLVLATDG VGTKLKIAQQ LGKHDTVGID LVAMCNNDIL 900
CNGAEPLTFL DYFACGKLDV NVATNVVSGI AEGCRQSDST LLGGETAEMP 950
GMYNPNVYDL AGFSLGVAEH EDILPKKNCL EVGDIIIGFP SNGVHSNGFS 1000
LIHKLFELTG YKWTDIAPFS AYGKTFGEEF LEPTKVYVKE ISPALKTGYV 1050
KALAHITGGG LWDNIPRVLP YNLTAELDAK KINISPVFAW LSLNGNIDKL 1100
ELLKTFNCGI GMIMIASKEH ELEILKSLYG SRASVIGKII PTKPHGHQVI 1150
VRHFATCFER VERLLSIPKK RVGVLISGSG SNLQALIDAT KSTNMGMCSE 1200
IVFVLSNKAG IFGLERAAKA NIPSTVISNK DYATREAFDV ALHNELIKHN 1250
VEIICLAGFM RILTPCFVNK WKGKLLNIHP SLLPKYKGIT AQKDALESGD 1300
NESGCTVHFV DENVDTGAII VQEIVPIFEN DTVESLTERI HVAEHIAFPK 1350
ALRLVASGYV RLNDKCETEW A 1371
Length:1,371
Mass (Da):149,103
Last modified:November 1, 1996 - v1
Checksum:i7BF4664DB1538946
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S43653 Genomic DNA. Translation: AAB23115.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S43653 Genomic DNA. Translation: AAB23115.1 .

3D structure databases

ProteinModelPortali Q26255.
SMRi Q26255. Positions 494-792.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00125 .
UPA00074 ; UER00126 .
UPA00074 ; UER00129 .

Family and domain databases

Gene3Di 3.30.1330.10. 2 hits.
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. 2 hits.
HAMAPi MF_00138. GARS.
InterProi 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 ]
Pfami PF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
PF00551. Formyl_trans_N. 1 hit.
PF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF53328. SSF53328. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsi TIGR00877. purD. 1 hit.
TIGR00878. purM. 2 hits.
TIGR00639. PurN. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Unusual organizational features of the Drosophila Gart locus are not conserved within Diptera."
    Clark D.V., Henikoff S.
    J. Mol. Evol. 35:51-59(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPUR2_CHITE
AccessioniPrimary (citable) accession number: Q26255
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi