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P96771 (PURA_AGGAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifier714 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Protein attributes

Sequence length259 AA.
Sequence statusFragment.
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
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

Chain‹1 – 259›259Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000095139

Regions

Nucleotide binding3 – 97GTP By similarity
Nucleotide binding31 – 333GTP By similarity
Region4 – 74IMP binding By similarity

Sites

Active site41Proton acceptor By similarity
Active site321Proton donor By similarity
Metal binding41Magnesium By similarity
Metal binding311Magnesium; via carbonyl oxygen By similarity
Binding site1201IMP By similarity
Binding site1341IMP; shared with dimeric partner By similarity
Binding site2151IMP By similarity
Binding site2301IMP By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P96771 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: E64198443875D6C6

FASTA25928,479
        10         20         30         40         50         60 
QWGDEGKGKI VDLLTDRVKY VVRYQGGRGA GHTLILNGEK TVLRLIPSGI LRDNVTCLIG 

        70         80         90        100        110        120 
NGVVLSPAAL MQEMSELENR GVNVRDRLLI SEACPLILPY HVAMDHAREA RWAKRPIRAT 

       130        140        150        160        170        180 
GRGIGPAYED KVARRGLRVG DLFDRAAFAE KLKNILDYYN FQLVNYYKVE PVDYQKTLDD 

       190        200        210        220        230        240 
VFAVADIITG MVADITTILD TARKNGDNIL FEGAQGTMLD IDHGTYPYVT SSNTAGGVAS 

       250 
GSGFGPRNLD YVLGIIKAY 

« Hide

References

[1]"Codon usage in Actinobacillus actinomycetemcomitans."
Kaplan J.B., Fine D.H.
FEMS Microbiol. Lett. 163:31-36(1998) [PubMed: 9631542] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CU1000.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89525 Genomic DNA. Translation: AAC46412.1.

3D structure databases

ProteinModelPortalP96771.
SMRP96771. Positions 1-259.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA_AGGAC
AccessionPrimary (citable) accession number: P96771
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: May 31, 2011
This is version 69 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