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P57629 (PURA_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BU566
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length433 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: 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 – 433433Adenylosuccinate synthetase HAMAP-Rule MF_00011
PRO_0000095157

Regions

Nucleotide binding13 – 197GTP By similarity
Nucleotide binding41 – 433GTP By similarity
Nucleotide binding332 – 3343GTP By similarity
Nucleotide binding414 – 4163GTP By similarity
Region14 – 174IMP binding By similarity
Region39 – 424IMP binding By similarity
Region300 – 3067Substrate binding By similarity

Sites

Active site141Proton acceptor By similarity
Active site421Proton donor By similarity
Metal binding141Magnesium By similarity
Metal binding411Magnesium; via carbonyl oxygen By similarity
Binding site1301IMP By similarity
Binding site1441IMP; shared with dimeric partner By similarity
Binding site2251IMP By similarity
Binding site2401IMP By similarity
Binding site3041IMP By similarity
Binding site3061GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
P57629 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: DB1C153C56851D05

FASTA43348,719
        10         20         30         40         50         60 
MNKNIVILGT QWGDEGKGKV VDCLTKDSSY VVRYQGGHNA GHTLVVNDKK IILHLIPSGL 

        70         80         90        100        110        120 
LHKNVIGIIA NGVVVSPFEL IKEIKMLETH NIFVHKRLFI SNSSPLILQY HIEMDIAREK 

       130        140        150        160        170        180 
KLGISALGTT GRGIGPAYED KIARRALRIG DLKNEKTLSI RLEKIVNYYN HQLVSFYKHK 

       190        200        210        220        230        240 
PVDYKIILRD LLPTIDLIYD MIKDTTSILH TAIQSNKKII FEGAQGSFLD IDHGTYPYVT 

       250        260        270        280        290        300 
SSNSTIGGVI TGTGVGSKSL DYILGVTKAY STRVGYGPFP TELFDDVDKH FSKKGHEFGS 

       310        320        330        340        350        360 
TTGRKRRTGW LDAVALCRSV RINSLSGLCI TKLDVLDGLH EIKICTAYKN INTLEIISFP 

       370        380        390        400        410        420 
DIDEWKNIEP IYETYPGWNK KTLGIKKLID LPYEARNYIN RIEEITQIPV DIISTGPDRS 

       430 
DIIFVRDIFF IKK

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000003 Genomic DNA. Translation: BAB13256.1.
RefSeqNP_240370.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57629.
SMRP57629. Positions 2-430.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB13256; BAB13256; BAB13256.
GeneID1109906.
KEGGbuc:BU566.
PATRIC21244676. VBIBucAph127364_0569.

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHOG000260959.
KOK01939.
OMADYVVRYQ.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-566-MONOMER.
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.
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_BUCAI
AccessionPrimary (citable) accession number: P57629
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: May 29, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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