P85910 (ASSY_PSEMZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Argininosuccinate synthase, chloroplastic EC=6.3.4.5 Alternative name(s): Citrulline--aspartate ligase
Organism	Pseudotsuga menziesii (Douglas-fir) (Abies menziesii)
Taxonomic identifier	3357 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Coniferophyta › Coniferopsida › Coniferales › Pinaceae › Pseudotsuga

Protein attributes

Sequence length	18 AA.
Sequence status	Fragments.
Protein existence	Evidence 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	Plastid › chloroplast By similarity UniProtKB Q9SZX3.
Sequence similarities	Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Chloroplast Plastid
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW argininosuccinate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›18	›18	Argininosuccinate synthase, chloroplastic		PRO_0000347323
Experimental info
	Non-adjacent residues	6 – 7	2
	Non-terminal residue	1	1
	Non-terminal residue	18	1

Sequences

	Sequence		Length	Mass (Da)
	P85910 [UniParc]. Last modified September 2, 2008. Version 1. Checksum: 94CF2BBCBF7C58F5	FASTA	18	2,065
	10 WFDPLRITET TTGSVTLK

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
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00068; UER00113.
Family and domain databases
PROSITE	PS00564. ARGININOSUCCIN_SYN_1. Partial match. PS00565. ARGININOSUCCIN_SYN_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASSY_PSEMZ

Accession

Primary (citable) accession number: P85910

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	September 2, 2008
Last modified:	January 9, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program