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Q5JIE6 (PURA_PYRKO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. 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:TK1002
OrganismPyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Thermococcus kodakaraensis (strain KOD1))
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

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_0000095278

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
Q5JIE6 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: AB497C2A8A5D6C45

FASTA33937,351
        10         20         30         40         50         60 
MPSYIVVGGQ WGDEGKGSVI AYLALKDEPE VIARGGVGTN AGHSVFINGK KYAVRQLPTG 

        70         80         90        100        110        120 
FMQTKARLLV GAGVLVDPEV FFHELEHLKD FNVRGRVGID YRCAIIEEKH KQLDRSNHHL 

       130        140        150        160        170        180 
HEEIGTTGSG CGPANADRVM RRAKLAKDIK ELEPYLTDVA AEVNDALDDG KLVLIEGTQG 

       190        200        210        220        230        240 
FGLSLYYGTY PYVTSKDTTA SAIASDVGIG PTRVDDVIVV FKSFPTRVGA GPFPTEMPQE 

       250        260        270        280        290        300 
EAERLGLVEY GTVTGRRRRV GWFDFEFARY SARINGATML ALTMLDKYDG EAFGVTDYDK 

       310        320        330 
LPKRAKEFVE EIEERVGVPV GLIKTGPELE HVIDRRENI

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed: 15710748] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006878 Genomic DNA. Translation: BAD85191.1.
RefSeqYP_183415.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JIE6.
SMRQ5JIE6. Positions 1-337.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000006410; EBPYRP00000006191; EBPYRG00000006409.
GeneID3234315.
GenomeReviewsGene locus TK1002 in contig AP006878_GR.
KEGGtko:TK1002.
NMPDRfig|69014.3.peg.1003.

Phylogenomic databases

eggNOGarNOG04146.
GeneTreeEBGT00050000023069.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBQ5JIE6.
ProtClustDBPRK04293.

Enzyme and pathway databases

BioCycTKOD69014:TK1002-MONOMER.

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. 2 hits.
[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_PYRKO
AccessionPrimary (citable) accession number: Q5JIE6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 15, 2005
Last modified: December 14, 2011
This is version 54 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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