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P65896 (PUR2_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:SA0926
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 1 magnesium or manganese ion 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 BAB42171.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Phosphoribosylamine--glycine ligase HAMAP-Rule MF_00138
PRO_0000151480

Regions

Domain108 – 311204ATP-grasp
Nucleotide binding134 – 19158ATP By similarity

Sites

Metal binding2811Magnesium or manganese By similarity
Metal binding2831Magnesium or manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
P65896 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 2F4A9770D6AA2523

FASTA41545,836
        10         20         30         40         50         60 
MNVLVIGAGG REHALAYKLN QSNLVKQEFV IPGNEAMTPI AEVHTEISES NHQGILDFAK 

        70         80         90        100        110        120 
QQNVDWVVIG PEQPLIDGLA DILRANGFKV FGPNKQAAQI EGSKLFAKKI MKKYNIPTAD 

       130        140        150        160        170        180 
YKEVERKKDA LTYIENCELP VVVKKDGLAA GKGVIIADTI EAARSAIEIM YGDEEEGTVV 

       190        200        210        220        230        240 
FETFLEGEEF SLMTFVNGDL AVPFDCIAQD HKRAFDHDEG PNTGGMGAYC PVPHISDDVL 

       250        260        270        280        290        300 
KLTNETIAQP IAKAMLNEGY QFFGVLYIGA ILTKDGPKVI EFNARFGDPE AQVLLSRMES 

       310        320        330        340        350        360 
DLMQHIIDLD EGKRTEFKWK NESIVGVMLA SKGYPDAYEK GHKVSGFDLN ENYFVSGLKK 

       370        380        390        400        410 
QGDTFVTSGG RVILAIGKGD NVQDAQRDAY EKVSQIQSDH LFYRHDIANK ALQLK 

« Hide

References

[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB42171.1. Different initiation.
PIRH89876.
RefSeqNP_374193.1. NC_002745.2.

3D structure databases

ProteinModelPortalP65896.
SMRP65896. Positions 1-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA0926.

Proteomic databases

PRIDEP65896.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB42171; BAB42171; BAB42171.
GeneID1123749.
KEGGsau:SA0926.
PATRIC19574040. VBIStaAur116463_0990.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0151.
HOGENOMHOG000033463.
KOK01945.
OrthoDBEOG69SKD1.
ProtClustDBPRK13790.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-978-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_STAAN
AccessionPrimary (citable) accession number: P65896
Secondary accession number(s): Q99V23
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 69 of the entry and version 1 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