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Reviewed, UniProtKB/Swiss-Prot Q46QQ8 (PURA2_RALEJ)

Last modified June 16, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase 2
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase 2
    AdSS 2
    AMPSase 2
Gene names
Name: purA2
Ordered Locus Names: Reut_B5180
OrganismRalstonia eutropha (strain JMP134) (Alcaligenes eutrophus) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. 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.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP 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 processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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 – 452452Adenylosuccinate synthetase 2 HAMAP MF_00011
PRO_0000224313

Sites

Metal binding201Magnesium By similarity
Metal binding471Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46QQ8-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 2FBB70A36A01F41D

FASTA45248,972
        10         20         30         40         50         60 
MDTATKTGYA DVLVGLQYGD EGKARVVDHL AAGYDVIARF NGGANAGHTI ATSEGILRLR 

        70         80         90        100        110        120 
QVPSGVLHPR VSLYIGSGCV IGLRQLASEI EMLAGQGIDL AGRLTISDRC PVVQPAHFLS 

       130        140        150        160        170        180 
DRRDGGRIGT TGNGIGPCYA DLAARMRGGE RSAFQLCDLM RDESRVFEQM MRLAAQRDDE 

       190        200        210        220        230        240 
DIAVLIQEMR QAWQVVRPFV TDNPVALLER VEGGARVLFE GAQSVMLDVV QGAQPWVTSS 

       250        260        270        280        290        300 
HTLPSYAYVG GDLPCRYHRK TIGVAKAMVS RVGSGPLPTE LGAERSEAYC ADAGREGRGR 

       310        320        330        340        350        360 
ADEAARFDPR ALLAQGDAFS TGIAIRMLSN EYGTGTGRPR RVGLLDVAQL QLAIRQFGVD 

       370        380        390        400        410        420 
EVYLNKCDSL AVFAQTRDRC IPVVVGSRDG NAMHVMRFPA FDESVIPRDD ATPLPPQLET 

       430        440        450 
LLEWLADVLG RPLRGIGLGP QRAQMRLFKT QP 

« Hide

References

[1]"Complete sequence of chromosome 2 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000091 Genomic DNA. Translation: AAZ64526.1.
RefSeqYP_299370.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3614614.
GenomeReviewsGene locus Reut_B5180 in contig CP000091_GR.
KEGGreu:Reut_B5180.
NMPDRfig|264198.3.peg.6155.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ46QQ8.
OMAQ46QQ8. LFEGAQS.

Enzyme and pathway databases

BioCycREUT264198:REUT_B5180-MON.

Family and domain databases

HAMAPMF_00011. Divergent sequence.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
ProDomPD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. False negative.
PS00513. ADENYLOSUCCIN_SYN_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA2_RALEJ
AccessionPrimary (citable) accession number: Q46QQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents