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O27494 (PUR2_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribosylamine--glycine ligase

EC=6.3.4.13
Alternative name(s):
GARS
Glycinamide ribonucleotide synthetase
Phosphoribosylglycinamide synthetase
Gene names
Name:purD
Ordered Locus Names:MTH_1445
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. HAMAP-Rule MF_00138

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathway

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. HAMAP-Rule MF_00138

Sequence similarities

Belongs to the GARS family.

Contains 1 ATP-grasp domain.

Sequence caution

The sequence AAB85920.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Phosphoribosylamine--glycine ligase HAMAP-Rule MF_00138
PRO_0000151513

Regions

Domain106 – 318213ATP-grasp
Nucleotide binding133 – 19664ATP By similarity
Compositional bias44 – 496Poly-Leu HAMAP-Rule MF_00138

Sites

Metal binding2761Magnesium or manganese 1 By similarity
Metal binding2881Magnesium or manganese 1 By similarity
Metal binding2881Magnesium or manganese 2 By similarity
Metal binding2901Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O27494 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: DF36C512561D354D

FASTA43647,882
        10         20         30         40         50         60 
MKILVVGTGA REHAICSALA DEATIYSVMG NRNPGISRLA GNSLLLLKLT PKVVRFASEK 

        70         80         90        100        110        120 
GVDMAFIGPE AHLEAGLVDA LEEAGIPSVG PTRDAARIET DKSFMRKLFE DYRIPGSITY 

       130        140        150        160        170        180 
RVFSDPEELR EFMEDFDSEA VVKPVGLTGG KGVKIVGEHL RDNMEALKYA TEVIEKRIGG 

       190        200        210        220        230        240 
HPSVVIEERV VGEEFTVQAF SDGEHIVPMP AVQDHPHAYE GDQGPITGGM GSYSDSDGLL 

       250        260        270        280        290        300 
PFLTQKDYED AVEIMQRTVD AIRKETGPYR GILYGQFMLS ADGPKLIEYN ARFGDPEAMN 

       310        320        330        340        350        360 
VLPLLESSML EICEGIVDGN LKSASFMNLA TVCKYLVPEG YPESGVAGAE IKVDEKKIED 

       370        380        390        400        410        420 
MGVITYYAAV NQEDDHIYTS SSRALALVAP ADDIYSAEEL CEEATAHVKG RLYHRRDIGT 

       430 
RELVEKRIKH MEDLRS 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85920.1. Different initiation.
PIRD69059.
RefSeqNP_276559.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH1445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85920; AAB85920; MTH_1445.
GeneID1471714.
KEGGmth:MTH1445.

Phylogenomic databases

eggNOGCOG0151.
KOK01945.
OMADPEAMNV.
ProtClustDBPRK00885.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1447-MONOMER.
UniPathwayUPA00074; UER00125.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.600.10. 1 hit.
HAMAPMF_00138. GARS.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
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.
[Graphical view]
PfamPF01071. GARS_A. 1 hit.
PF02843. GARS_C. 1 hit.
PF02844. GARS_N. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR00877. purD. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUR2_METTH
AccessionPrimary (citable) accession number: O27494
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways