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Q8U3Z2 (PURA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PF0308
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length339 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
Reference 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 – 339339Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095276

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding42 – 443GTP By similarity
Nucleotide binding284 – 2863GTP By similarity
Nucleotide binding324 – 3263GTP By similarity
Region13 – 164IMP binding By similarity
Region40 – 434IMP binding By similarity
Region252 – 2587Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site431Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding421Magnesium; via carbonyl oxygen By similarity
Binding site1271IMP By similarity
Binding site1411IMP; shared with dimeric partner By similarity
Binding site1791IMP By similarity
Binding site1941IMP By similarity
Binding site2561IMP By similarity
Binding site2581GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8U3Z2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 1740E55D3A46F71A

FASTA33937,135
        10         20         30         40         50         60 
MPSVIVVGGQ WGDEGKGSII AYLALHDEPE IIARGGVGTN AGHSVVINGK KYAVRQLPTG 

        70         80         90        100        110        120 
FMQTKARLLV GAGVLVDPEV FFYELEHLKD FNVAERVGID YRCAIIEPKH KEMDRKNDYL 

       130        140        150        160        170        180 
HGTIGTTGSG CGPANADRVM RVAKQAKDIK ELEPYLTDVA AEVNDALDEG ALVLVEGTQG 

       190        200        210        220        230        240 
FGLSLYYGTY PYVTSKDTTA SAVASDVGIG PTRVDDVIVV FKSFPTRVGA GPFPTEMPME 

       250        260        270        280        290        300 
EADRLGLIEY GTVTGRRRRV GWFDFEMARY AARINGATML AVTMLDKYDK EAFGITDYDK 

       310        320        330 
LPRKAKEFIE EIEERVGVPV GLIKTGPELE HIIDLRENI

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009950 Genomic DNA. Translation: AAL80432.1.
RefSeqNP_578037.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U3Z2.
SMRQ8U3Z2. Positions 1-337.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000005898; EBPYRP00000005759; EBPYRG00000005897.
GeneID1468143.
GenomeReviewsGene locus PF0308 in contig AE009950_GR.
KEGGpfu:PF0308.
NMPDRfig|186497.1.peg.314.

Phylogenomic databases

GeneTreeEBGT00050000023069.
HOGENOMHBG658237.
OMAYVLGIIK.
ProtClustDBPRK04293.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[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]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_PYRFU
AccessionPrimary (citable) accession number: Q8U3Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 61 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

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