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Q8NYX6 (PURA_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase
Short name=AMPSase
Short name=AdSS
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase
Gene names
Name:purA
Ordered Locus Names:MW0017
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_00011

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_00011

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000095231

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding330 – 3323GTP By similarity
Nucleotide binding412 – 4143GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region298 – 3047Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site411Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity
Binding site1281IMP By similarity
Binding site1421IMP; shared with dimeric partner By similarity
Binding site2231IMP By similarity
Binding site2381IMP By similarity
Binding site3021IMP By similarity
Binding site3041GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NYX6 [UniParc].

Last modified October 19, 2002. Version 1.
Checksum: A65C1C7140B0FCCE

FASTA42747,579
        10         20         30         40         50         60 
MSSIVVVGTQ WGDEGKGKIT DFLAEQSDVI ARFSGGNNAG HTIQFGGETY KLHLVPSGIF 

        70         80         90        100        110        120 
YKDKLAVIGN GVVVDPVALL KELDGLNERG IPTSNLRISN RAQVILPYHL AQDEYEERLR 

       130        140        150        160        170        180 
GDNKIGTTKK GIGPAYVDKV QRIGIRMADL LEKETFERLL KSNIEYKQAY FKGMFNETCP 

       190        200        210        220        230        240 
SFDDIFEEYY AAGQRLKEFV TDTSKILDDA FVADEKVLFE GAQGVMLDID HGTYPFVTSS 

       250        260        270        280        290        300 
NPIAGNVTVG TGVGPTFVSK VIGVCKAYTS RVGDGPFPTE LFDEDGHHIR EVGREYGTTT 

       310        320        330        340        350        360 
GRPRRVGWFD SVVLRHSRRV SGITDLSINS IDVLTGLDTV KICTAYELDG KEITEYPANL 

       370        380        390        400        410        420 
DQLKRCKPIF EELPGWTEDV TNVRTLEELP ENARKYLERI SELCNVQISI FSVGPDREQT 


NLLKELW

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000033 Genomic DNA. Translation: BAB93882.1.
RefSeqNP_644832.1. NC_003923.1.

3D structure databases

ProteinModelPortalQ8NYX6.
SMRQ8NYX6. Positions 2-425.
ModBaseSearch...

Protein-protein interaction databases

STRING196620.MW0017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB93882; BAB93882; BAB93882.
GeneID1004402.
KEGGsam:MW0017.
PATRIC19566466. VBIStaAur44266_0017.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-17-MONOMER.
UniPathwayUPA00075; UER00335.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_STAAW
AccessionPrimary (citable) accession number: Q8NYX6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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