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Q7N8D4 (PURA1_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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 1

Short name=AMPSase 1
Short name=AdSS 1
EC=6.3.4.4
Alternative name(s):
IMP--aspartate ligase 1
Gene names
Name:purA1
Ordered Locus Names:plu0794
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length419 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
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 – 419419Adenylosuccinate synthetase 1 HAMAP MF_00011
PRO_0000095207

Regions

Nucleotide binding11 – 177GTP By similarity
Nucleotide binding326 – 3283GTP By similarity
Nucleotide binding407 – 4093GTP By similarity
Region12 – 154IMP binding By similarity
Region37 – 404IMP binding By similarity
Region294 – 3007Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Active site401Proton donor By similarity
Metal binding121Magnesium By similarity
Metal binding391Magnesium; via carbonyl oxygen By similarity
Binding site1381IMP; shared with dimeric partner By similarity
Binding site2201IMP By similarity
Binding site2981IMP By similarity
Binding site3001GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N8D4 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 7191F44A4E238351

FASTA41946,976
        10         20         30         40         50         60 
MLTAVVGLQF GDEGKGKFVD YLSGNINNIA RFNGGANAGH CVQHGNLRGS FSQLPASLNK 

        70         80         90        100        110        120 
KNLYICQGAL ISLPILVKEI DFIKKEDIDS HIFIDPRCHI VLPLHAELNR ASEKYKGKQK 

       130        140        150        160        170        180 
IGSVGVGVGA CVEDKANRHG IRLIDTFDKE KLRSKLEFLW SIREKQINHV FNAQASLDFE 

       190        200        210        220        230        240 
EMLETTHQYG KRIEPYFTFT NEIIGDLLNS GEDVLLETSQ ATFLDNSFGT YPYTVAYQTL 

       250        260        270        280        290        300 
VQTCFAMIGI PAQKMHIVGV MKSYMIRVGN GPFPTELSTE QADYIRERGN EYGTVSKRPR 

       310        320        330        340        350        360 
RCGWLDLSLI KHAVKLNGVI ELAITNVDVL AGLDEIKVAV AYEIDDKLVC CDNALLQLDR 

       370        380        390        400        410 
AKPIYKTFKS WSTLNSSYTD LTELPIELID FLSFIQDYTG VPIKYISYGP DRNQTLVVK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571861 Genomic DNA. Translation: CAE13089.1.
RefSeqNP_928139.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N8D4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2800757.
GenomeReviewsGene locus plu0794 in contig BX470251_GR.
KEGGplu:plu0794.
NMPDRfig|243265.1.peg.763.
PATRIC20505199. VBIPhoLum48522_0873.

Organism-specific databases

GenoListplu0794.
CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMARERGNEY.
PhylomeDBQ7N8D4.
ProtClustDBCLSK2521706.

Enzyme and pathway databases

BioCycPLUM243265:PLU0794-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]
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA1_PHOLL
AccessionPrimary (citable) accession number: Q7N8D4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 59 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