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Q6MN06 (PURA_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Bd1460
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [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. 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

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

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 By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding333 – 3353GTP By similarity
Nucleotide binding415 – 4173GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region301 – 3077Substrate 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 site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2261IMP By similarity
Binding site2411IMP By similarity
Binding site3051IMP By similarity
Binding site3071GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MN06 [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 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842649 Genomic DNA. Translation: CAE79346.1.
RefSeqNP_968353.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MN06.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2735591.
GenomeReviewsGene locus Bd1460 in contig BX842601_GR.
KEGGbba:Bd1460.
NMPDRfig|264462.1.peg.1323.
PATRIC21077488. VBIBdeBac73187_1321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMADYVVRYQ.
PhylomeDBQ6MN06.

Enzyme and pathway databases

BioCycBBAC264462:BD1460-MONOMER.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth. Divergent sequence.
[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. 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: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families