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Database: UniProt
Entry: Q5ZJ23
LinkDB: Q5ZJ23
Original site: Q5ZJ23 
ID   ASSY_CHICK              Reviewed;         416 AA.
AC   Q5ZJ23;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   07-JUN-2017, entry version 84.
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=RCJMB04_21j5 {ECO:0000312|EMBL:CAG32270.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: One of the enzymes of the urea cycle, the metabolic
CC       pathway transforming neurotoxic amonia produced by protein
CC       catabolism into inocuous urea in the liver of ureotelic animals.
CC       Catalyzes the formation of arginosuccinate from aspartate,
CC       citrulline and ATP and together with ASL it is responsible for the
CC       biosynthesis of arginine in most body tissues.
CC       {ECO:0000250|UniProtKB:P00966}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC       diphosphate + N(omega)-(L-arginino)succinate.
CC       {ECO:0000250|UniProtKB:P00966}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine 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}.
DR   EMBL; AJ720611; CAG32270.1; -; mRNA.
DR   RefSeq; NP_001013413.1; NM_001013395.1.
DR   UniGene; Gga.5385; -.
DR   ProteinModelPortal; Q5ZJ23; -.
DR   SMR; Q5ZJ23; -.
DR   STRING; 9031.ENSGALP00000006379; -.
DR   PaxDb; Q5ZJ23; -.
DR   GeneID; 417185; -.
DR   KEGG; gga:417185; -.
DR   CTD; 445; -.
DR   eggNOG; KOG1706; Eukaryota.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   HOVERGEN; HBG001717; -.
DR   InParanoid; Q5ZJ23; -.
DR   KO; K01940; -.
DR   PhylomeDB; Q5ZJ23; -.
DR   UniPathway; UPA00068; UER00113.
DR   UniPathway; UPA00158; UER00272.
DR   PRO; PR:Q5ZJ23; -.
DR   Proteomes; UP000000539; 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; IDA:AgBase.
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   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;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Urea cycle.
FT   CHAIN         1    416       Argininosuccinate synthase.
FT                                /FTId=PRO_0000321322.
FT   NP_BIND      11     19       ATP. {ECO:0000250|UniProtKB:P00966}.
FT   NP_BIND     116    124       ATP. {ECO:0000250|UniProtKB:P00966}.
FT   BINDING      37     37       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250|UniProtKB:P00966}.
FT   BINDING      88     88       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     120    120       Aspartate.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     124    124       Aspartate.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     124    124       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     125    125       Aspartate.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     128    128       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     181    181       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     190    190       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     271    271       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   BINDING     283    283       Citrulline.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   MOD_RES      88     88       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P09034}.
FT   MOD_RES     114    114       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P00966}.
FT   MOD_RES     181    181       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00966}.
SQ   SEQUENCE   416 AA;  46904 MW;  AF0CC73CA67D1B71 CRC64;
     MAEPRDTVVL AYSGGLDTSC ILVWLKEQGY TVIAFLANIG QTEDFDAAQK KALALGAKKV
     YIQDVCREFV EDFIWPAVRA NALYEDRYML GSALARPCIA RHLVLIAQEE GARYIAHGAT
     GKGNDQVRFE LGCYALCPSI KVIAPWRMPE FYQRFPGRRE LMEYAQKHGI PVPVTPKAPW
     SMDENLMHIS YEAGILENPK NRAPLDLYTK TCNPTTSPDV PDELEIEFEK GVPVKVTNTR
     NGVTHRSALE LFVYLNDIAS KHGVGRVDIV ENRFVGMKSR GIYETPAGTI LYHAHLDIEA
     FTMDREVRKI KQGLSLKFSE LVYNGFWYSP ECEFLKHCIA RSQQAVAGTV HVSVFKGQVY
     VLGRESPHSL YNEELVSMDV QGDYEPADAT GFININALRL KEYHRLQSKV STKQDE
//
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