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O67321 (PURA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. 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:aq_1290
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length432 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 – 432432Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095142

Regions

Nucleotide binding12 – 187GTP By similarity
Nucleotide binding40 – 423GTP By similarity
Nucleotide binding328 – 3303GTP By similarity
Nucleotide binding410 – 4123GTP By similarity
Region13 – 164IMP binding By similarity
Region38 – 414IMP binding By similarity
Region296 – 3027Substrate binding By similarity

Sites

Active site131Proton acceptor By similarity
Active site411Proton donor By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity
Binding site1261IMP By similarity
Binding site1401IMP; shared with dimeric partner By similarity
Binding site2191IMP By similarity
Binding site2341IMP By similarity
Binding site3001IMP By similarity
Binding site3021GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
O67321 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: ACA52CE913DE62E7

FASTA43248,854
        10         20         30         40         50         60 
MEKLIILGAQ WGDEGKGKIV DLLSEHFDIT VRYQGGSNAG HTVVVNSQKF ILHLLPTGIL 

        70         80         90        100        110        120 
HEHVKGVIAQ GMVVDLEVLH KEVKNLEEKG IYVKERLFIS DRAHLVMPYH KLLDSLFEKK 

       130        140        150        160        170        180 
KGIGTTLRGI GPAYMFKYGR KGIRISDLKD EKRFYTLLED NLDFVKNICE KVFCEKFDLD 

       190        200        210        220        230        240 
INQIYEEQLR YFEEFKENVV DLLRFFNTQK GSVLFEGAQG TLLDVDMGTY PYVTSSNASA 

       250        260        270        280        290        300 
LGLSNGTGMP PKYFSDAFFL GVAKAYTTRV GEGPFPTELK GEEGEKLREL GGEYGSTTGR 

       310        320        330        340        350        360 
PRRCGWLDLV ALKYAVQVNG LDGFVITKLD VLDTFDEVKV CVAYELDGEV IDYFPASYSE 

       370        380        390        400        410        420 
LIRVKPVYKT LKGWKKSTKG AKDVSELPKE ALDYVKFIEE YTGVPVVMLS TGPKRDEYIW 

       430 
LKEILRTRSG YS

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC07286.1.
PIRF70411.
RefSeqNP_213885.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67321.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192759.
GenomeReviewsGene locus aq_1290 in contig AE000657_GR.
KEGGaae:aq_1290.
NMPDRfig|224324.1.peg.900.
PATRIC20959784. VBIAquAeo85532_1009.

Phylogenomic databases

HOGENOMHBG658237.
OMADYVVRYQ.
PhylomeDBO67321.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1290-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. 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_AQUAE
AccessionPrimary (citable) accession number: O67321
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 82 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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