ASSY_DANRE
ID ASSY_DANRE Reviewed; 414 AA.
AC Q66I24;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
GN ORFNames=zgc:92051 {ECO:0000312|EMBL:AAH81578.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2007) 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; BC081578; AAH81578.1; -; mRNA.
DR EMBL; BC154282; AAI54283.1; -; mRNA.
DR RefSeq; NP_001004603.1; NM_001004603.1.
DR AlphaFoldDB; Q66I24; -.
DR SMR; Q66I24; -.
DR STRING; 7955.ENSDARP00000039902; -.
DR PaxDb; Q66I24; -.
DR GeneID; 447864; -.
DR KEGG; dre:447864; -.
DR CTD; 445; -.
DR ZFIN; ZDB-GENE-040912-178; ass1.
DR eggNOG; KOG1706; Eukaryota.
DR InParanoid; Q66I24; -.
DR OrthoDB; 1459745at2759; -.
DR PhylomeDB; Q66I24; -.
DR UniPathway; UPA00068; UER00113.
DR UniPathway; UPA00158; UER00272.
DR PRO; PR:Q66I24; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0000053; P:argininosuccinate metabolic process; IBA:GO_Central.
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..414
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000321323"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 86
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 91
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 114..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 118
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 122
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 122
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 126
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 179
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 188
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 269
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 281
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
SQ SEQUENCE 414 AA; 47129 MW; A75FD4D9CD0611D3 CRC64;
MSKGLVVLAY SGGLDTSCIL VWLKEQGYDV IAYLANIGQD EDFDVARKKA EKLGAKKVFI
EDLRSEFVQE FIWPALQANA LYEDRYLLGT SIARPCIARR QVQIAQREGA QYVSHGATGK
GNDQVRFELT CYALYPQVQV IAPWRIPEFY NRFRGRKDLM EYAEKHNIPV PVTPKAPWSM
DANLMHISYE SGILENPKNH APSDLYQMTK NPEHSPDQAD MLEIEFKKGV PVRVSHLKDG
ISKETPLEIF CYLNEIGGKH GVGRIDIVEN RFIGMKSRGI YETPGGTVLL QAHLDIETFT
MDREVRKIKQ SLGIKFSELI YNGFWFSPEC EFVRECVERS QKHVEGRVQL SVYKGQVYIL
GRESPKSLYN EELVSMDVQG DYDPCDASGF IKINAVRLRE HNRLQGAALS KHNV
