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Q57981 (PURA_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. 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:MJ0561
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length345 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
Reference 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 – 345345Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000095271

Regions

Nucleotide binding18 – 247GTP By similarity
Nucleotide binding48 – 503GTP By similarity
Nucleotide binding290 – 2923GTP By similarity
Nucleotide binding330 – 3323GTP By similarity
Region19 – 224IMP binding By similarity
Region46 – 494IMP binding By similarity
Region258 – 2647Substrate binding By similarity

Sites

Active site191Proton acceptor By similarity
Active site491Proton donor By similarity
Metal binding191Magnesium By similarity
Metal binding481Magnesium; via carbonyl oxygen By similarity
Binding site1331IMP By similarity
Binding site1471IMP; shared with dimeric partner By similarity
Binding site1851IMP By similarity
Binding site2001IMP By similarity
Binding site2621IMP By similarity
Binding site2641GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57981 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9974DBC30D1DEE72

FASTA34537,820
        10         20         30         40         50         60 
MKKVVLLTCT IIVGGQWGDE GKGKIISYIC DKDKPSIIAR GGVGPNAGHT VNIGGKSYGI 

        70         80         90        100        110        120 
RMIPTGFPYK EAKLAIGAGV LVDPEVLLKE VEMLKDFNVK ERLIVDYRCG IIEEKHKIMD 

       130        140        150        160        170        180 
RKDEHLAKEI GTTGSGCGPA NVDRVLRILK QAKDIEELKE FLGDVSEEVN NALDRGENVL 

       190        200        210        220        230        240 
IEGTQGTLLS LYYGTYPYVT SKDTTASSFA ADVGIGPTKV DEVIVVFKTF PTRVGAGPFP 

       250        260        270        280        290        300 
TEMSLEEAES LGIVEYGTVT GRRRRVGYFD FELARKACRL NGATQIALTG LDKYDKECYG 

       310        320        330        340 
VTEYNKLSEK AKEFINKIEE VTGVPVTIIS TGPEMHQTID LRNEL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98554.1.
PIRA64370.
RefSeqNP_247540.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ57981.
SMRQ57981. Positions 11-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98554; AAB98554; MJ_0561.
GeneID1451426.
KEGGmja:MJ_0561.

Phylogenomic databases

eggNOGCOG0104.
KOK01939.
OMADYVVRYQ.
ProtClustDBPRK04293.

Enzyme and pathway databases

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.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_METJA
AccessionPrimary (citable) accession number: Q57981
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 98 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names