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Reviewed, UniProtKB/Swiss-Prot B4UGW9 (PURA_ANASK)

Last modified November 3, 2009. Version 10. 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: AnaeK_2598
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis By similarity.

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.

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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_1000089267

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1411 By similarity
Active site1481 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B4UGW9-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: EC6474364F80A360

FASTA43246,711
        10         20         30         40         50         60 
MPNVVVVGAQ WGDEGKGKIV DLLTQYADVV VRFQGGNNAG HTLVVGGEKT VLHLIPSGIL 

        70         80         90        100        110        120 
HPGKSCVIGN GVVIDPEVLV LEIDRLKAKG ALKDDGQLVV SLDAHVIMPW HKAIDVAREQ 

       130        140        150        160        170        180 
AMGEGKIGTT GRGIGPTYED KVARRGLRIR DLLDEARLAR KVKERAALAR EELARLGAKL 

       190        200        210        220        230        240 
ELDEPALVKR YAELGRRVSG YATDVSIWLH RALQQGKSLL FEGAQGTMLD VDHGTYPFVT 

       250        260        270        280        290        300 
SSNTVAGNAV VGCGLGPTAV DYVLGISKAY STRVGGGPYP TELKDETGER LRKLGGEYGA 

       310        320        330        340        350        360 
TTGRPRRTGW LDALALRYAV RVNGLSGIAM TKLDVLTGFD TVKIAVGYRL DGKVLDEMPS 

       370        380        390        400        410        420 
DPEVIERCTP VYEELPGWTE KLEHLRTWDD LPPRARAYVK RVEELAGVKV VGCSVGADRG 

       430 
ETILVENPFL AR 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. K."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001131 Genomic DNA. Translation: ACG73823.1.
RefSeqYP_002134952.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6787026.
GenomeReviewsGene locus AnaeK_2598 in contig CP001131_GR.
KEGGank:AnaeK_2598.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYVLGIIK.

Family and domain databases

HAMAPMF_00011.
[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...

Entry information

Entry namePURA_ANASK
AccessionPrimary (citable) accession number: B4UGW9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 10 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