Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7NS98 (PURA2_CHRVO)

Last modified February 9, 2010. Version 54. 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

Hide | Top

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: CV_3528
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Hide | Top

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

Hide | Top

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. 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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Adenylosuccinate synthetase 2 HAMAP MF_00011
PRO_0000095166

Regions

Nucleotide binding13 – 197GTP Potential

Sites

Active site1411 By similarity
Active site1481 By similarity
Metal binding141Magnesium By similarity
Metal binding411Magnesium; via carbonyl oxygen By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q7NS98-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 373EE33F255E64BB

FASTA43146,638
        10         20         30         40         50         60 
MSKNVVVIGT QWGDEGKGKI VDWLTDHARA VVRFQGGHNA GHTLWVNGKK TVVRLVPSGI 

        70         80         90        100        110        120 
LRPDVECFIG NGVVLSPEAL LKEIDELEAA GVNASARLKI AEGCPLILPY HIALDQAREA 

       130        140        150        160        170        180 
AKGDAKIGTT GRGIGPCYED KVARRALKVI DLFDPARFET KLKENVDYYN FLLTNLFKAE 

       190        200        210        220        230        240 
PVSYEAILAD TMKMAERIKP MVADVSRTLY DLDKAGTPIL FEGAQGTLLD IDHGTYPYVT 

       250        260        270        280        290        300 
SSNCVAGAAA PGAGVPPQML NYVLGIVKGY ATRVGSGPFP TEQENEIGAF LAKRGNEFGS 

       310        320        330        340        350        360 
VTGRPRRCGW FDAAALKRSI QINGVSGLCV MKLDVMDGLE EIKLCTGYML DGQKVDILPF 

       370        380        390        400        410        420 
GSDAVTKCEP VYETLPGWTG TTVGVKRWED LPANAQAYLK RIEEVCGAPV DIVSTGPDRE 

       430 
ETIVLRHPFG L

« Hide

Hide | Top

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ61190.1.
RefSeqNP_903198.1.

3D structure databases

SMRQ7NS98. Positions 4-429.
ModBaseSearch...

Genome annotation databases

GeneID2547652.
GenomeReviewsGene locus CV_3528 in contig AE016825_GR.
KEGGcvi:CV_3528.
NMPDRfig|243365.1.peg.3528.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ7NS98.

Enzyme and pathway databases

BioCycCVIO243365:CV_3528-MONOMER.
BRENDA6.3.4.4. 415.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth. Divergent sequence.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
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...

Hide | Top

Entry information

Entry namePURA2_CHRVO
AccessionPrimary (citable) accession number: Q7NS98
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 15, 2003
Last modified: February 9, 2010
This is version 54 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)

Hide | Top

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