Skip Header

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

Phosphoribosylamine--glycine ligase

Gene

purD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (purF)
  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
Metal bindingi286Magnesium or manganeseBy similarity1
Metal bindingi288Magnesium or manganeseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi135 – 196ATPBy similarityAdd BLAST62

GO - Molecular functioni

  • ATPase activity, coupled Source: EcoliWiki
  • ATP binding Source: EcoliWiki
  • metal ion binding Source: UniProtKB-KW
  • phosphoribosylamine-glycine ligase activity Source: EcoCyc

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • purine nucleobase biosynthetic process Source: InterPro
  • purine nucleotide biosynthetic process Source: EcoliWiki

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:GLYCRIBONUCSYN-MONOMER
MetaCyc:GLYCRIBONUCSYN-MONOMER
BRENDAi6.3.4.13 2026
UniPathwayiUPA00074; UER00125

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylamine--glycine ligase (EC:6.3.4.13)
Alternative name(s):
GARS
Glycinamide ribonucleotide synthetase
Phosphoribosylglycinamide synthetase
Gene namesi
Name:purD
Ordered Locus Names:b4005, JW3969
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10792 purD

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001514481 – 429Phosphoribosylamine--glycine ligaseAdd BLAST429

Proteomic databases

PaxDbiP15640
PRIDEiP15640

2D gel databases

SWISS-2DPAGEP15640

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262462, 50 interactors
IntActiP15640, 4 interactors
STRINGi316385.ECDH10B_4194

Structurei

Secondary structure

1429
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 7Combined sources7
Helixi10 – 19Combined sources10
Beta strandi25 – 32Combined sources8
Helixi35 – 39Combined sources5
Beta strandi43 – 45Combined sources3
Helixi53 – 62Combined sources10
Beta strandi66 – 70Combined sources5
Helixi73 – 77Combined sources5
Helixi80 – 86Combined sources7
Beta strandi91 – 93Combined sources3
Turni96 – 99Combined sources4
Helixi100 – 103Combined sources4
Helixi105 – 114Combined sources10
Beta strandi122 – 129Combined sources8
Helixi130 – 138Combined sources9
Beta strandi140 – 145Combined sources6
Beta strandi155 – 160Combined sources6
Helixi161 – 168Combined sources8
Turni169 – 172Combined sources4
Beta strandi184 – 188Combined sources5
Beta strandi192 – 204Combined sources13
Beta strandi206 – 219Combined sources14
Turni220 – 222Combined sources3
Beta strandi223 – 235Combined sources13
Helixi241 – 250Combined sources10
Helixi252 – 261Combined sources10
Beta strandi267 – 277Combined sources11
Beta strandi282 – 290Combined sources9
Turni293 – 295Combined sources3
Helixi296 – 302Combined sources7
Helixi307 – 315Combined sources9
Helixi319 – 321Combined sources3
Beta strandi328 – 338Combined sources11
Turni339 – 342Combined sources4
Beta strandi362 – 371Combined sources10
Beta strandi377 – 379Combined sources3
Beta strandi381 – 393Combined sources13
Helixi394 – 404Combined sources11
Turni405 – 407Combined sources3
Helixi421 – 425Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSOX-ray1.60A1-429[»]
ProteinModelPortaliP15640
SMRiP15640
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15640

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini109 – 316ATP-graspAdd BLAST208

Sequence similaritiesi

Belongs to the GARS family.Curated

Phylogenomic databases

eggNOGiENOG4105C12 Bacteria
COG0151 LUCA
HOGENOMiHOG000033463
InParanoidiP15640
KOiK01945
OMAiKATVCKY
PhylomeDBiP15640

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_sf
IPR020561 PRibGlycinamid_synth_ATP-grasp
IPR000115 PRibGlycinamide_synth
IPR020560 PRibGlycinamide_synth_C-dom
IPR037123 PRibGlycinamide_synth_C_sf
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.

P15640-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVLVIGNGG REHALAWKAA QSPLVETVFV APGNAGTALE PALQNVAIGV
60 70 80 90 100
TDIPALLDFA QNEKIDLTIV GPEAPLVKGV VDTFRAAGLK IFGPTAGAAQ
110 120 130 140 150
LEGSKAFTKD FLARHKIPTA EYQNFTEVEP ALAYLREKGA PIVIKADGLA
160 170 180 190 200
AGKGVIVAMT LEEAEAAVHD MLAGNAFGDA GHRIVIEEFL DGEEASFIVM
210 220 230 240 250
VDGEHVLPMA TSQDHKRVGD KDTGPNTGGM GAYSPAPVVT DDVHQRTMER
260 270 280 290 300
IIWPTVKGMA AEGNTYTGFL YAGLMIDKQG NPKVIEFNCR FGDPETQPIM
310 320 330 340 350
LRMKSDLVEL CLAACESKLD EKTSEWDERA SLGVVMAAGG YPGDYRTGDV
360 370 380 390 400
IHGLPLEEVA GGKVFHAGTK LADDEQVVTN GGRVLCVTAL GHTVAEAQKR
410 420
AYALMTDIHW DDCFCRKDIG WRAIEREQN
Length:429
Mass (Da):45,940
Last modified:October 1, 1993 - v2
Checksum:i5E9EFAD478BC1FF4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15 – 16LA → WR in AAA24455 (PubMed:2687276).Curated2
Sequence conflicti97G → V in AAA24455 (PubMed:2687276).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05126 Genomic DNA Translation: AAA24455.1
X51950 Genomic DNA Translation: CAA36213.1
U00006 Genomic DNA Translation: AAC43103.1
U00096 Genomic DNA Translation: AAC76979.1
AP009048 Genomic DNA Translation: BAE77314.1
PIRiA33771 AJECQG
RefSeqiNP_418433.1, NC_000913.3
WP_000866800.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76979; AAC76979; b4005
BAE77314; BAE77314; BAE77314
GeneIDi948504
KEGGiecj:JW3969
eco:b4005
PATRICifig|1411691.4.peg.2705

Similar proteinsi

Entry informationi

Entry nameiPUR2_ECOLI
AccessioniPrimary (citable) accession number: P15640
Secondary accession number(s): Q2M8U2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1993
Last modified: March 28, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health