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B3R989 (B3R989_CUPTR) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 26. 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 2 HAMAP MF_00011
Short name=AMPSase 2 HAMAP MF_00011
Short name=AdSS 2 HAMAP MF_00011
EC=6.3.4.4 HAMAP MF_00011
Alternative name(s):
IMP--aspartate ligase 2 HAMAP MF_00011
Gene names
Name:purAlike EMBL CAQ71464.1
Synonyms:purA2 HAMAP MF_00011
Ordered Locus Names:RALTA_B0848
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length459 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 MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP MF_00011 RuleBase RU000520

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 RuleBase RU000520

Subunit structure

Homodimer By similarity. HAMAP MF_00011

Subcellular location

Cytoplasm By similarity HAMAP MF_00011.

Sequence similarities

Belongs to the adenylosuccinate synthetase family. HAMAP MF_00011 RuleBase RU004163

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding19 – 257GTP By similarity HAMAP MF_00011
Nucleotide binding47 – 493GTP By similarity HAMAP MF_00011
Nucleotide binding368 – 3703GTP By similarity HAMAP MF_00011
Nucleotide binding440 – 4423GTP By similarity HAMAP MF_00011
Region20 – 234IMP binding By similarity HAMAP MF_00011
Region45 – 484IMP binding By similarity HAMAP MF_00011
Region336 – 3427Substrate binding By similarity HAMAP MF_00011

Sites

Active site201Proton acceptor By similarity HAMAP MF_00011
Active site481Proton donor By similarity HAMAP MF_00011
Metal binding201Magnesium By similarity HAMAP MF_00011
Metal binding471Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1311IMP By similarity HAMAP MF_00011
Binding site1451IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site2251IMP By similarity HAMAP MF_00011
Binding site2401IMP By similarity HAMAP MF_00011
Binding site3401IMP By similarity HAMAP MF_00011
Binding site3421GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
B3R989 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 4EA266B4B1639C97

FASTA45948,550
        10         20         30         40         50         60 
MGAATKTGYA DVLVGLQFGD EGKARIVDHL AAGYDVIARF NGGANAGHTI ATPSGALRLR 

        70         80         90        100        110        120 
QVPSGVLHPG VALYIGSGCV VGLQQLASEI AMLAAQGISL EGRLTISDRC PLVQPRHVLA 

       130        140        150        160        170        180 
DRRDGARIGT TGNGIGPCYA DLAARMRGAE RVAFQLRDLW CDEGRVFELM TRLASQADDD 

       190        200        210        220        230        240 
DEAIAAMVDG MRHAWRVVRP FVTNDAVALL RRVEAGARVL FEGAQSVMLD VVHGVQPWVT 

       250        260        270        280        290        300 
SSHTLPAYAY VGGDLPCRYH RKTIGVAKAI VSRVGNGPLP TELGGQRSEA YCAAAAHAGR 

       310        320        330        340        350        360 
GRADEAASHD PLKLLAEADA FSTGVAIRML ANEYGTGTGR PRRVGLLDVA QLQRAIQQAG 

       370        380        390        400        410        420 
VDEVYLNKCD SLAAFSHTPE RCIPVIVAGE AGSASQRVLQ FPAFAHGSIP TDAASPLPPQ 

       430        440        450 
LEALLAWLAH AIGRPLRGIG LGPERAQMRL LEPNQQTTP

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References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633750 Genomic DNA. Translation: CAQ71464.1.
RefSeqYP_002007521.1. NC_010530.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3R989.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6455514.
GenomeReviewsGene locus RALTA_B0848 in contig CU633750_GR.
KEGGcti:RALTA_B0848.
PATRIC21535471. VBICupTai42494_4345.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMALFEGAQS.
ProtClustDBCLSK939171.

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]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB3R989_CUPTR
AccessionPrimary (citable) accession number: B3R989
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: December 14, 2011
This is version 26 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