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 03-APR-2013, entry version 61.
DE RecName: Full=Argininosuccinate synthase;
DE EC=6.3.4.5;
DE AltName: Full=Citrulline--aspartate ligase;
GN Name=ASS1; ORFNames=RCJMB04_21j5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; 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 -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC diphosphate + N(omega)-(L-arginino)succinate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-
CC arginino)succinate from L-aspartate and L-citrulline: step 1/1.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family.
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DR EMBL; AJ720611; CAG32270.1; -; mRNA.
DR IPI; IPI00598406; -.
DR RefSeq; NP_001013413.1; NM_001013395.1.
DR UniGene; Gga.5385; -.
DR HSSP; P59846; 1J20.
DR ProteinModelPortal; Q5ZJ23; -.
DR SMR; Q5ZJ23; 5-408.
DR STRING; 9031.ENSGALP00000006379; -.
DR PaxDb; Q5ZJ23; -.
DR GeneID; 417185; -.
DR KEGG; gga:417185; -.
DR CTD; 445; -.
DR eggNOG; COG0137; -.
DR HOGENOM; HOG000230093; -.
DR HOVERGEN; HBG001717; -.
DR InParanoid; Q5ZJ23; -.
DR KO; K01940; -.
DR OrthoDB; EOG45B1FK; -.
DR UniPathway; UPA00068; UER00113.
DR UniPathway; UPA00158; UER00272.
DR NextBio; 20820530; -.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 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; Ligase; Nucleotide-binding; Reference proteome;
KW Urea cycle.
FT CHAIN 1 416 Argininosuccinate synthase.
FT /FTId=PRO_0000321322.
FT NP_BIND 11 19 ATP (By similarity).
FT NP_BIND 116 124 ATP (By similarity).
FT BINDING 37 37 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 88 88 Citrulline (By similarity).
FT BINDING 120 120 Aspartate (By similarity).
FT BINDING 124 124 Aspartate (By similarity).
FT BINDING 124 124 Citrulline (By similarity).
FT BINDING 125 125 Aspartate (By similarity).
FT BINDING 128 128 Citrulline (By similarity).
FT BINDING 181 181 Citrulline (By similarity).
FT BINDING 190 190 Citrulline (By similarity).
FT BINDING 271 271 Citrulline (By similarity).
FT BINDING 283 283 Citrulline (By similarity).
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
//
