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Protein

Phosphoribosylamine--glycine ligase

Gene

purD

Organism
Streptococcus suis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 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 (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF), Amidophosphoribosyltransferase (purF)
  2. Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), Phosphoribosylamine--glycine ligase (purD), 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
Metal bindingi284Magnesium or manganeseUniRule annotation1
Metal bindingi286Magnesium or manganeseUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi134 – 195ATPUniRule annotationAdd BLAST62

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00125.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylamine--glycine ligaseUniRule annotation (EC:6.3.4.13UniRule annotation)
Alternative name(s):
GARSUniRule annotation
Glycinamide ribonucleotide synthetaseUniRule annotation
Phosphoribosylglycinamide synthetaseUniRule annotation
Gene namesi
Name:purDUniRule annotation
OrganismiStreptococcus suis
Taxonomic identifieri1307 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001514931 – 420Phosphoribosylamine--glycine ligaseAdd BLAST420

Structurei

3D structure databases

ProteinModelPortaliQ9F1S9.
SMRiQ9F1S9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini108 – 314ATP-graspUniRule annotationAdd BLAST207

Sequence similaritiesi

Belongs to the GARS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C12. Bacteria.
COG0151. LUCA.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.90.600.10. 1 hit.
HAMAPiMF_00138. GARS. 1 hit.
InterProiView protein in InterPro
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
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.
IPR011054. Rudment_hybrid_motif.
PfamiView protein in Pfam
PF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
SMARTiView protein in SMART
SM01210. GARS_C. 1 hit.
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00877. purD. 1 hit.
PROSITEiView protein in PROSITE
PS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9F1S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLVVGSGG REHAIAKKLL ESEQVEQVFV APGNDGMTLD GIELINIGIS
60 70 80 90 100
EHSALINFAK ENDIAWTFVG PDDALAAGIV DDFEQAGLKA FGPSRLAAEL
110 120 130 140 150
EWSKDFAKQI MVKYGIPTAA FGTFSNFEEA KAYIEEQGAP IVVKADGLAL
160 170 180 190 200
GKGVVVAETV EQAVEAAREM LLDNKFGDSG ARVVIEEFLA GEEFSLFALV
210 220 230 240 250
NGDQFYILPT AQDHKRAFDG DQGPNTGGMG AYVHVPHLPQ SVVDTAVDTI
260 270 280 290 300
VKPILEGMIT EGRSYLGVLY AGLILTDQGP KVIEFNARFG DPETQIILPR
310 320 330 340 350
LTSDFAQNID DILHKRPTQL TWLNSGVTLG VVVASNGYPL DYEKGVTLPA
360 370 380 390 400
KTEGDITTYY AGARFAENSR ALLSNGGRVY MLVTTADTVQ DAQEKIYSEL
410 420
KNQDTTGLFY RTDIGSKAVK
Length:420
Mass (Da):45,333
Last modified:March 1, 2001 - v1
Checksum:i14E9C2D29CDF6B9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045609 Genomic DNA. Translation: BAB20832.1.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPUR2_STRSU
AccessioniPrimary (citable) accession number: Q9F1S9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2001
Last modified: July 5, 2017
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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