ID   ASSY_PSEMZ              Reviewed;          18 AA.
AC   P85910;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Argininosuccinate synthase, chloroplastic {ECO:0000250|UniProtKB:Q9SZX3};
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000250|UniProtKB:Q9SZX3};
DE   Flags: Fragments;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC         arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:456215; EC=6.3.4.5;
CC         Evidence={ECO:0000250|UniProtKB:Q9SZX3};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000250|UniProtKB:Q9SZX3}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9SZX3}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:Q9SZX3}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC       subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P85910; -.
DR   UniPathway; UPA00068; UER00113.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Chloroplast;
KW   Ligase; Nucleotide-binding; Plastid.
FT   CHAIN           <1..>18
FT                   /note="Argininosuccinate synthase, chloroplastic"
FT                   /id="PRO_0000347323"
FT   NON_CONS        6..7
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         18
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   18 AA;  2065 MW;  94CF2BBCBF7C58F5 CRC64;
     WFDPLRITET TTGSVTLK