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B4EPF9 (B4EPF9_BURCJ) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 25. 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:purA2 HAMAP MF_00011
Ordered Locus Names:BceJ2315_70240
ORF Names:BCAS0771 EMBL CAR57705.1
OrganismBurkholderia cepacia (strain J2315 / LMG 16656) (Burkholderia cenocepacia (strain J2315)) [Complete proteome] [HAMAP] EMBL CAR57705.1
Taxonomic identifier216591 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length432 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. RuleBase RU004163 HAMAP MF_00011

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding12 – 187GTP By similarity HAMAP MF_00011
Nucleotide binding40 – 423GTP By similarity HAMAP MF_00011
Nucleotide binding329 – 3313GTP By similarity HAMAP MF_00011
Nucleotide binding411 – 4133GTP By similarity HAMAP MF_00011
Region13 – 164IMP binding By similarity HAMAP MF_00011
Region38 – 414IMP binding By similarity HAMAP MF_00011
Region297 – 3037Substrate binding By similarity HAMAP MF_00011

Sites

Active site131Proton acceptor By similarity HAMAP MF_00011
Active site411Proton donor By similarity HAMAP MF_00011
Metal binding131Magnesium By similarity HAMAP MF_00011
Metal binding401Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1281IMP By similarity HAMAP MF_00011
Binding site1421IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site2221IMP By similarity HAMAP MF_00011
Binding site2371IMP By similarity HAMAP MF_00011
Binding site3011IMP By similarity HAMAP MF_00011
Binding site3031GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
B4EPF9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 67487E0903C212F4

FASTA43245,782
        10         20         30         40         50         60 
MPNVVVVGAQ WGDEGKGRVV DWLAAQADLV ARYNGGHNAG HTLVVGGNTY KLALLPSGIV 

        70         80         90        100        110        120 
RGKRGVIGNG VALDPEALLA EIGRMAELGL SVTPDNLSIA ENATLVLPIH RAIDEAQERL 

       130        140        150        160        170        180 
RREPIGTTLR GIGPAYEDKV GRRGLRVGDL AEPGGLAAKL DVLVDHHNAW FRGLGLDAYD 

       190        200        210        220        230        240 
RDAMLATLVA LAPKILPFVR PVWADLNDAT DRGERILFEG SQAVMLDIDW GTYPFVTSSG 

       250        260        270        280        290        300 
TVASAAAAGT GLGAAKLGHV LGVTKAYATR VGGGPFLTEL TDATGETLRA RGQEFGVNTG 

       310        320        330        340        350        360 
RPRRCGWLDA AQLRQAVRIS GIDSFALTKL DVLDGFESID LCVGYEFDGA RVDHLPASLD 

       370        380        390        400        410        420 
AQSRAKPVYE RFEGWQGSVK GVRERAALPR AARDFIARIE TVAGAPVSMI TTGAERDDTI 

       430 
VLRNPFDAAG AA

« Hide

References

[1]"Genomic analysis of Burkholderia cenocepacia J2315, an epidemic cystic fibrosis pathogen."
Holden M.T.G.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM747722 Genomic DNA. Translation: CAR57705.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4EPF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus BceJ2315_70240 in contig AM747722_GR.
KEGGbcj:BCAS0771.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAPIHRAID.
ProtClustDBCLSK941367.

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 nameB4EPF9_BURCJ
AccessionPrimary (citable) accession number: B4EPF9
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: November 16, 2011
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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