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Q2G1S3 (Q2G1S3_STAA8) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 57. Feed History...

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

Protein namesRecommended name:
Adenylosuccinate synthetase HAMAP-Rule MF_00011
Short name=AMPSase HAMAP-Rule MF_00011
Short name=AdSS HAMAP-Rule MF_00011
EC=6.3.4.4 HAMAP-Rule MF_00011
Alternative name(s):
IMP--aspartate ligase HAMAP-Rule MF_00011
Gene names
Name:purA HAMAP-Rule MF_00011
Ordered Locus Names:SAOUHSC_00019
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP] EMBL ABD29208.1
Taxonomic identifier93061 [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 By similarity. RuleBase RU000520

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited 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. RuleBase RU000520 HAMAP-Rule MF_00011

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00011

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. RuleBase RU000520 HAMAP-Rule MF_00011

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00011

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family. RuleBase RU000520 HAMAP-Rule MF_00011

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding12 – 187GTP By similarity HAMAP-Rule MF_00011
Nucleotide binding40 – 423GTP By similarity HAMAP-Rule MF_00011
Nucleotide binding330 – 3323GTP By similarity HAMAP-Rule MF_00011
Nucleotide binding412 – 4143GTP By similarity HAMAP-Rule MF_00011
Region13 – 164IMP binding By similarity HAMAP-Rule MF_00011
Region38 – 414IMP binding By similarity HAMAP-Rule MF_00011
Region298 – 3047Substrate binding By similarity HAMAP-Rule MF_00011

Sites

Active site131Proton acceptor By similarity HAMAP-Rule MF_00011
Active site411Proton donor By similarity HAMAP-Rule MF_00011
Metal binding131Magnesium By similarity HAMAP-Rule MF_00011
Metal binding401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_00011
Binding site1281IMP By similarity HAMAP-Rule MF_00011
Binding site1421IMP; shared with dimeric partner By similarity HAMAP-Rule MF_00011
Binding site2231IMP By similarity HAMAP-Rule MF_00011
Binding site2381IMP By similarity HAMAP-Rule MF_00011
Binding site3021IMP By similarity HAMAP-Rule MF_00011
Binding site3041GTP By similarity HAMAP-Rule MF_00011

Sequences

Sequence LengthMass (Da)Tools
Q2G1S3 [UniParc].

Last modified March 21, 2006. 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

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References

[1]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000253 Genomic DNA. Translation: ABD29208.1.
RefSeqYP_498625.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2G1S3.
SMRQ2G1S3. Positions 2-425.
ModBaseSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00019.

PTM databases

PhosSiteP0909761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD29208; ABD29208; SAOUHSC_00019.
GeneID3919190.
KEGGsao:SAOUHSC_00019.
PATRIC19577678. VBIStaAur99865_0017.

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-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 nameQ2G1S3_STAA8
AccessionPrimary (citable) accession number: Q2G1S3
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2006
Last sequence update: March 21, 2006
Last modified: May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info