ASSY_XENLA
ID ASSY_XENLA Reviewed; 411 AA.
AC Q7ZWM4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Argininosuccinate synthase {ECO:0000305};
DE EC=6.3.4.5 {ECO:0000250|UniProtKB:P00966};
DE AltName: Full=Citrulline--aspartate ligase;
GN Name=ass1 {ECO:0000250|UniProtKB:P00966};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway
CC transforming neurotoxic amonia produced by protein catabolism into
CC inocuous urea in the liver of ureotelic animals. Catalyzes the
CC formation of arginosuccinate from aspartate, citrulline and ATP and
CC together with ASL it is responsible for the biosynthesis of arginine in
CC most body tissues. {ECO:0000250|UniProtKB:P00966}.
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:P00966};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 2/3.
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-
CC arginino)succinate from L-aspartate and L-citrulline: step 1/1.
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00966}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family.
CC {ECO:0000305}.
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DR EMBL; BC046941; AAH46941.1; -; mRNA.
DR RefSeq; NP_001080795.1; NM_001087326.1.
DR AlphaFoldDB; Q7ZWM4; -.
DR SMR; Q7ZWM4; -.
DR PRIDE; Q7ZWM4; -.
DR DNASU; 380488; -.
DR GeneID; 380488; -.
DR KEGG; xla:380488; -.
DR CTD; 380488; -.
DR Xenbase; XB-GENE-17340606; ass1.L.
DR OrthoDB; 1459745at2759; -.
DR UniPathway; UPA00068; UER00113.
DR UniPathway; UPA00158; UER00272.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 380488; Expressed in camera-type eye and 15 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004055; F:argininosuccinate synthase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0000050; P:urea cycle; ISS:UniProtKB.
DR CDD; cd01999; Argininosuccinate_Synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 1.
DR HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR InterPro; IPR001518; Arginosuc_synth.
DR InterPro; IPR018223; Arginosuc_synth_CS.
DR InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
DR InterPro; IPR024074; AS_cat/multimer_dom_body.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11587; PTHR11587; 1.
DR Pfam; PF00764; Arginosuc_synth; 1.
DR SUPFAM; SSF69864; SSF69864; 1.
DR TIGRFAMs; TIGR00032; argG; 1.
DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome; Urea cycle.
FT CHAIN 1..411
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000321324"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 88
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 93
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 116..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 120
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 124
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 124
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 125
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 128
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 181
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 190
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 271
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 283
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
SQ SEQUENCE 411 AA; 46750 MW; 9A9F683A38A2378C CRC64;
MSQSKGTVVL AYSGGLDTSC ILVWLKEQGF DVIAYLANIG QNEDFEEARK KAVNLGAKKV
YIEDIRQQFV EEYIWPAVQA NAIYEDRYLL GTSLARPCIA KKQVEIAKKE AAEYVSHGAT
GKGNDQIRFE LTCYSLYPEV KIIAPWRMPE FYNRFRGRSD LMEYAKKHNI SVPVTPKSPW
SMDENLMHIS YEGGILENPK NHAPPGLYLK TKDPATSPDE PDILEIEFKK GVPVKVTNTK
NKTQHSSSLA LFCYLNEVAG KHGVGRIDIV ENRFIGMKSR GIYETPAGTI LYQAHLDIEA
FTMDREMRKI KQQLSQRFAE QIYNGFWYSP ECEFVRSCIS KSQEMVEGKV LVSVLKGQVY
VLGREAPHSL YNEELVSMDV QGDYDPADAC GFIKINAVRL KEYHRLQKNK K
