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Protein

Amidophosphoribosyltransferase

Gene

purF

Organism
Dialister invisus DSM 15470
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.UniRule annotation

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit.UniRule annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (GCWU000321_00717)
  2. Phosphoribosylamine--glycine ligase (purD)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei17For GATase activityUniRule annotation1
Active sitei17NucleophileUniRule annotation1
Metal bindingi251Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi298MagnesiumUniRule annotation1
Metal bindingi360MagnesiumUniRule annotation1
Metal bindingi361MagnesiumUniRule annotation1
Metal bindingi397Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi449Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi452Iron-sulfur (4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferaseUniRule annotationImported, Transferase
Biological processPurine biosynthesisUniRule annotation
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, MagnesiumUniRule annotation, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
AmidophosphoribosyltransferaseUniRule annotation (EC:2.4.2.14UniRule annotation)
Short name:
ATaseUniRule annotation
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferaseUniRule annotation
Short name:
GPATaseUniRule annotation
Gene namesi
Name:purFUniRule annotationImported
ORF Names:GCWU000321_00798Imported
OrganismiDialister invisus DSM 15470Imported
Taxonomic identifieri592028 [NCBI]
Taxonomic lineageiBacteriaFirmicutesNegativicutesVeillonellalesVeillonellaceaeDialister
Proteomesi
  • UP000004736 Componenti: Unassembled WGS sequence

Interactioni

Protein-protein interaction databases

STRINGi592028.GCWU000321_00798.

Structurei

3D structure databases

ProteinModelPortaliC9LMP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 234Glutamine amidotransferase type-2InterPro annotationAdd BLAST218

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferaseUniRule annotation

Phylogenomic databases

eggNOGiENOG4105CBA. Bacteria.
COG0034. LUCA.
OrthoDBiPOG091H0061.

Family and domain databases

CDDicd00715. GPATase_N. 1 hit.
cd06223. PRTases_typeI. 1 hit.
Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF. 1 hit.
InterProiView protein in InterPro
IPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
IPR035584. PurF_N.
PfamiView protein in Pfam
PF13537. GATase_7. 1 hit.
PF00156. Pribosyltran. 1 hit.
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiView protein in PROSITE
PS51278. GATASE_TYPE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

C9LMP4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDGNMAACD DKFHEECGVF AIYDRNRPAA LETYYGVFSL QHRGQESAGI
60 70 80 90 100
TVSDGHTMET FRGMGLVTEV FRKLPEKEGF IGIGHVRYST TGSSIPSNIQ
110 120 130 140 150
PLQLEGAEGP LALAHNGNLV NTKVLRNRLL QSGSTFQTTM DTEIIIKLLA
160 170 180 190 200
HAGAAVMEDR IKGVMDEIRG AYAVVACTNQ AVYGFRDPFG YRPMALGKTE
210 220 230 240 250
SGYVLCSETP ALDAIDAEFV RDILPGEIVR IDDDGVHSTM YGKKAPRLGI
260 270 280 290 300
CAFEYIYFAR PDSVMNGQDI YEARLSMGRH LWEETHYEGD VVMSVPDSGN
310 320 330 340 350
VAALGYSHAS GIPYVEGLLK NKYMGRTFIQ PGQKQRERAV RMKLNPIVMN
360 370 380 390 400
VKGKRIILVD DSIVRGTTSG IIIRLLRNAG AKEIKMCISS PPVRFPCFFG
410 420 430 440 450
IDTAQRRQLV AASHSEEEIC KMIGADKLHY LSQKGLAESI SRIRAKDMCF
460 470
ACFDGDYPEP VSGGGLDGMK E
Length:471
Mass (Da):51,836
Last modified:November 24, 2009 - v1
Checksum:iDD2BB1ED1819F8FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACIM02000001 Genomic DNA. Translation: EEW96830.1.

Genome annotation databases

EnsemblBacteriaiEEW96830; EEW96830; GCWU000321_00798.

Similar proteinsi

Entry informationi

Entry nameiC9LMP4_9FIRM
AccessioniPrimary (citable) accession number: C9LMP4
Entry historyiIntegrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: September 27, 2017
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

Complete proteomeImported