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Protein

Argininosuccinate synthase, chloroplastic

Gene
N/A
Organism
Pseudotsuga menziesii (Douglas-fir) (Abies menziesii)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. argininosuccinate synthase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthase, chloroplasticBy similarity (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligaseBy similarity
OrganismiPseudotsuga menziesii (Douglas-fir) (Abies menziesii)
Taxonomic identifieri3357 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePseudotsuga

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›18›18Argininosuccinate synthase, chloroplasticPRO_0000347323Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 1 subfamily.Sequence Analysis

Sequencei

Sequence statusi: Fragments.

P85910-1 [UniParc]FASTAAdd to Basket

« Hide

        10 
WFDPLRITET TTGSVTLK
Length:18
Mass (Da):2,065
Last modified:September 2, 2008 - v1
Checksum:i94CF2BBCBF7C58F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 111 Publication
Non-adjacent residuesi6 – 721 Publication
Non-terminal residuei18 – 1811 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiASSY_PSEMZ
AccessioniPrimary (citable) accession number: P85910
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 7, 2015
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.