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B0R4U8 (PURA_HALS3) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:OE2579F
OrganismHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) [Complete proteome] [HAMAP]
Taxonomic identifier478009 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length440 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 – 440440Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000089299

Regions

Nucleotide binding11 – 177GTP By similarity
Nucleotide binding39 – 413GTP By similarity
Nucleotide binding339 – 3413GTP By similarity
Nucleotide binding424 – 4263GTP By similarity
Region12 – 154IMP binding By similarity
Region37 – 404IMP binding By similarity
Region307 – 3137Substrate 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 site1271IMP By similarity
Binding site1411IMP; shared with dimeric partner By similarity
Binding site2301IMP By similarity
Binding site2451IMP By similarity
Binding site3111IMP By similarity
Binding site3131GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0R4U8 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: FD36AE43C7344E4E

FASTA44047,110
        10         20         30         40         50         60 
MTVTIVGAQL GDEGKGGVVD LFGDATDVVV RYQGGDNAGH TVVAGGEEYK LSLVPSGVVR 

        70         80         90        100        110        120 
GKTGVLGNGC VINPETLFEE VDALRERGLD PDVRLAKRAH VILPFHRELD GAEEAAKADS 

       130        140        150        160        170        180 
DSEIGTTGRG IGPTYEDKIG RRGVRVGDLL NEDALRDRLE YLVDAKRAIY EDVYGFDASE 

       190        200        210        220        230        240 
TDGAFDIDAI HEQCLAYADR IRDEDLAVNA GDYLADRIAD GDNVMLEGAQ GTSLDIDHGN 

       250        260        270        280        290        300 
FPYVTSSNPT AGYAATGSGL GPTTVGQGEI VGIIKAYLSR VGSGPMPTEL DGDQAEYIRE 

       310        320        330        340        350        360 
EGGEYGTVTG RPRRVGWLDM PMLRHAARAN GFTGIAINHL DVLAELDEVN VGHAYERDGE 

       370        380        390        400        410        420 
RIHTLPATTE AWRDCDPVMK SFDGWSAFDP AVVADAGYSA LPDNAQAYVE YVEAELDTPA 

       430        440 
YVLGVGPGRE ESVIRQNPFE

« Hide

References

[1]"Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
Genomics 91:335-346(2008) [PubMed: 18313895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29341 / DSM 671 / R1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM774415 Genomic DNA. Translation: CAP13763.1.
RefSeqYP_001689111.1. NC_010364.1.

3D structure databases

ProteinModelPortalB0R4U8.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0R4U8.

Proteomic databases

PRIDEB0R4U8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5952824.
GenomeReviewsGene locus OE2579F in contig AM774415_GR.
KEGGhsl:OE2579F.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBB0R4U8.
ProtClustDBPRK13785.

Enzyme and pathway databases

BioCycHSAL478009:OE2579F-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_HALS3
AccessionPrimary (citable) accession number: B0R4U8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: December 14, 2011
This is version 30 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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