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Reviewed, UniProtKB/Swiss-Prot Q6MN06 (PURA_BDEBA)

Last modified February 9, 2010. Version 43. 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

Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AdSS
    AMPSase
Gene names
Name: purA
Ordered Locus Names: Bd1460
OrganismBdellovibrio bacteriovorus [Complete proteome] [HAMAP]
Taxonomic identifier959 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

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. 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: 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000224259

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1411 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MN06-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 94529BF30BE46BCB

FASTA43246,897
        10         20         30         40         50         60 
MSGVVVVGAQ WGDEGKGKLI DVFAEKADMV VRYQGGANAG HTLVVNGQKT VLHLVPSGIL 

        70         80         90        100        110        120 
RPETTCVIAS GVVIDVFSIR DEIKKLKDTG FLQNPKQLLI SDTATLILPY HKALDAAREA 

       130        140        150        160        170        180 
ALSDGKIGTT GKGIGPAYED RASRRAILFG DLFDKDNLKK KLELALTEKN FMLENYYKGS 

       190        200        210        220        230        240 
TFKADDLIKD LLAVAEELAP YRTKDTSLFI SKSLKSGKRV LFEGAQGTML DILHGTYPFV 

       250        260        270        280        290        300 
TSSSTLASNA CASAGIGPAS VQKVIGVFKA YTTRVGSGPF PTELNDEIGK KIQADGHEFG 

       310        320        330        340        350        360 
STTGRSRRCG WLDLVALKYA IRVNGITNLA MMKLDVLTGH DRIGVCTAYK LNGEIITDLP 

       370        380        390        400        410        420 
TSPYELEKVE PVIEWIPGWT QDLTKVKTLS DLPRPTTNYI DYLGSQLGTP IDVISVGPGR 

       430 
EQTLWVKPLF NN 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / HD100 / DSM 50701 / NCIB 9529.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842649 Genomic DNA. Translation: CAE79346.1.
RefSeqNP_968353.1.

3D structure databases

SMRQ6MN06. Positions 3-431.
ModBaseSearch...

Genome annotation databases

GeneID2735591.
KEGGbba:Bd1460.
NMPDRfig|264462.1.peg.1323.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAIPVCVAY.
PhylomeDBQ6MN06.

Enzyme and pathway databases

BioCycBBAC264462:BD1460-MONOMER.
BRENDA6.3.4.4. 3459.

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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_BDEBA
AccessionPrimary (citable) accession number: Q6MN06
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 43 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)

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