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P0C115 (PURA_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BruAb1_1668
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length429 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 committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_00011

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00011

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00011

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000095153

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 site1291IMP By similarity
Binding site1431IMP; 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
P0C115 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: DF90E83E30690FF2

FASTA42946,561
        10         20         30         40         50         60 
MANVVVVGSQ WGDEGKGKIV DWLSERADVI VRYQGGHNAG HTLVIDGVSY KLSLLPSGLV 

        70         80         90        100        110        120 
RGKLSVIGNG VVVDPHHFVA EVEKLRGQGI DVTPDVLRVA ENAPLILSIH RELDAMREGS 

       130        140        150        160        170        180 
NSGLKIGTTK RGIGPAYEDK VGRRAIRVID LTEPETLRPK VERLLAHHNS LRRGMGLEEI 

       190        200        210        220        230        240 
AVETILTELT SVADQILPYI DQVWRVLDER RKAGARILFE GAQGALLDND HGTYPFVTSS 

       250        260        270        280        290        300 
NTVAGQAAAG SGLGPTAIGY VLGITKAYTT RVGEGPFPTE LNDEIGEFLG TKGHEFGVVT 

       310        320        330        340        350        360 
GRKRRCGWFD AVIVRQTVRT SGINGIALTK LDVLDGLEEI KICVAYELDG KRIDYLPSSM 

       370        380        390        400        410        420 
GAQARVKPIY ETLPGWSETT AGARSWNDLP AQAVKYVRHI EELIGAPVAM LSTSPEREDT 


ILVTDPFHD 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX74987.1.
RefSeqYP_222348.1. NC_006932.1.

3D structure databases

ProteinModelPortalP0C115.
SMRP0C115. Positions 2-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb1_1668.

Proteomic databases

PRIDEP0C115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX74987; AAX74987; BruAb1_1668.
GeneID3340306.
KEGGbmb:BruAb1_1668.
PATRIC17825118. VBIBruAbo15061_1761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
OrthoDBEOG68Q0QG.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycBABO262698:GJC2-1708-MONOMER.
UniPathwayUPA00075; UER00335.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11846. PTHR11846. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_BRUAB
AccessionPrimary (citable) accession number: P0C115
Secondary accession number(s): P52004, Q57BJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names