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Q46QQ8 (PURA2_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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 2
Short name=AMPSase 2
Short name=AdSS 2
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase 2
Gene names
Name:purA2
Ordered Locus Names:Reut_B5180
OrganismCupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length452 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 – 452452Adenylosuccinate synthetase 2 HAMAP MF_00011
PRO_0000224313

Regions

Nucleotide binding19 – 257GTP By similarity
Nucleotide binding47 – 493GTP By similarity
Nucleotide binding366 – 3683GTP By similarity
Nucleotide binding437 – 4393GTP By similarity
Region20 – 234IMP binding By similarity
Region45 – 484IMP binding By similarity
Region334 – 3407Substrate binding By similarity

Sites

Active site201Proton acceptor By similarity
Active site481Proton donor By similarity
Metal binding201Magnesium By similarity
Metal binding471Magnesium; via carbonyl oxygen By similarity
Binding site1311IMP By similarity
Binding site1451IMP; shared with dimeric partner By similarity
Binding site2231IMP By similarity
Binding site2381IMP By similarity
Binding site3381IMP By similarity
Binding site3401GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46QQ8 [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].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000091 Genomic DNA. Translation: AAZ64526.1.
RefSeqYP_299370.1. NC_007348.1.

3D structure databases

ProteinModelPortalQ46QQ8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ46QQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3614614.
GenomeReviewsGene locus Reut_B5180 in contig CP000091_GR.
KEGGreu:Reut_B5180.
NMPDRfig|264198.3.peg.6155.
PATRIC20236285. VBIRalEut24049_5944.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMALFEGAQS.
ProtClustDBCLSK939171.

Enzyme and pathway databases

BioCycREUT264198:REUT_B5180-MONOMER.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth. Divergent sequence.
[Tree]
InterProIPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
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_CUPPJ
AccessionPrimary (citable) accession number: Q46QQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 45 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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