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Q4A164 (PURA_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:SSP0017
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteria › Firmicutes › 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 commited step in the biosynthesis of AMP from IMP By similarity. HAMAP MF_00011

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00011

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP MF_00011

Subcellular location

Cytoplasm By similarity HAMAP MF_00011.

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 processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000224323

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
Q4A164 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 9E6FE0954A8BBE90

FASTA42747,192
        10         20         30         40         50         60 
MSSIVVVGTQ WGDEGKGKIT DFLAEQADVI ARFSGGNNAG HTIKFGGETY KLHLVPSGIF 

        70         80         90        100        110        120 
YKEKLAVIGN GVVVDPVALL KELDALNERG ISTDNLRISN RAQVILPYHI KQDEYEEERR 

       130        140        150        160        170        180 
GDNKIGTTKK GIGPAYVDKA QRIGIRVADL LDKETFEKLL KDNIEYKGAY FEGMFGKACP 

       190        200        210        220        230        240 
TFEEIFETYY AAGQRLAQFV TDTAKVLDDA FVADEKVLFE GAQGVMLDID HGTYPFVTSS 

       250        260        270        280        290        300 
NPVAGNVTVG GGVGPTFVSK VIGVCKAYTS RVGDGPFPTE LFDEDGHHIR EVGREYGTTT 

       310        320        330        340        350        360 
GRPRRVGWFD SVVLRHSRRA SGITDLSINS IDVLTGLKEV KICTAYELDG KEITEYPANL 

       370        380        390        400        410        420 
KDLQRCKPIF ETLPGWTEDV TGCRSLEELP NNARRYLERI SELCDVKISI FSVGPDRNQT 


NLLKSLW

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed: 16135568] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008934 Genomic DNA. Translation: BAE17162.1.
RefSeqYP_300107.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ4A164.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4A164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000047340; EBSTAP00000045709; EBSTAG00000047337.
GeneID3615243.
GenomeReviewsGene locus SSP0017 in contig AP008934_GR.
KEGGssp:SSP0017.
NMPDRfig|342451.4.peg.96.
PATRIC19621511. VBIStaSap90642_0018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
GeneTreeEBGT00050000025160.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ4A164.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycSSAP342451:SSP0017-MONOMER.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
PANTHERPTHR11846. Asucc_synthtase. 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_STAS1
AccessionPrimary (citable) accession number: Q4A164
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 49 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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