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P85910 (ASSY_PSEMZ) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 14. 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:
Argininosuccinate synthase, chloroplastic

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
OrganismPseudotsuga menziesii (Douglas-fir) (Abies menziesii)
Taxonomic identifier3357 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePseudotsuga

Protein attributes

Sequence length18 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. UniProtKB Q9SZX3

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. UniProtKB Q9SZX3

Subunit structure

Homotetramer By similarity. UniProtKB Q9SZX3

Subcellular location

Plastidchloroplast By similarity UniProtKB Q9SZX3.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentChloroplast
Plastid
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›18›18Argininosuccinate synthase, chloroplastic
PRO_0000347323

Experimental info

Non-adjacent residues6 – 72
Non-terminal residue11
Non-terminal residue181

Sequences

Sequence LengthMass (Da)Tools
P85910 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 94CF2BBCBF7C58F5

FASTA182,065
        10 
WFDPLRITET TTGSVTLK 

« Hide

References

[1]"A proteomics approach to identify proteins differentially expressed in Douglas-fir seedlings infected by Phellinus sulphurascens."
Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.
J. Proteomics 71:425-438(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameASSY_PSEMZ
AccessionPrimary (citable) accession number: P85910
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: March 19, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways