ID   ASSY_AEDAE              Reviewed;         412 AA.
AC   Q0IFL5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   ORFNames=AAEL004701;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M.,
RA   Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J.,
RA   Sinkins S.P., Hogenkamp D.G., Amedeo P., Arensburger P.,
RA   Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V.,
RA   Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B.,
RA   DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M.,
RA   Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H.,
RA   Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S.,
RA   Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D.,
RA   Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A.,
RA   Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D.,
RA   White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A.,
RA   Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J.,
RA   Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B.,
RA   Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
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)succinic acid from L-aspartate and L-citrulline: step
CC       1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family.
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DR   EMBL; CH477312; EAT43888.1; -; Genomic_DNA.
DR   RefSeq; XP_001649600.1; -.
DR   UniGene; Aae.10323; -.
DR   GeneID; 5565274; -.
DR   KEGG; aag:AaeL_AAEL004701; -.
DR   VectorBase; AAEL004701; Aedes aegypti.
DR   OMA; Q0IFL5; IAPVREW.
DR   BRENDA; 6.3.4.5; 1026.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001518; Arginosuc_synth.
DR   InterPro; IPR018223; Arginosuc_synth_CS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11587; Arginosuc_synth; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW   Nucleotide-binding; Urea cycle.
FT   CHAIN         1    412       Argininosuccinate synthase.
FT                                /FTId=PRO_0000321326.
FT   NP_BIND      10     18       ATP (By similarity).
FT   NP_BIND     115    123       ATP (By similarity).
FT   BINDING      36     36       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING      87     87       Citrulline (By similarity).
FT   BINDING      92     92       Citrulline (By similarity).
FT   BINDING     119    119       Aspartate (By similarity).
FT   BINDING     123    123       Aspartate (By similarity).
FT   BINDING     123    123       Citrulline (By similarity).
FT   BINDING     124    124       Aspartate (By similarity).
FT   BINDING     127    127       Citrulline (By similarity).
FT   BINDING     180    180       Citrulline (By similarity).
FT   BINDING     189    189       Citrulline (By similarity).
FT   BINDING     270    270       Citrulline (By similarity).
FT   BINDING     282    282       Citrulline (By similarity).
SQ   SEQUENCE   412 AA;  45989 MW;  BB9595CF2605F70F CRC64;
     MSGKEKILLA YSGGLDTSCI LKWLLEKGYE VICFMADVGQ EEDFVAAREK ALRVGAKDVI
     IKDMKRIFVE KFVWPAIQMG LVYEDRYLLG TSLARPCISI GLMESAAEHS CSIISHGATG
     KGNDQIRFEL SCYALDPKIK VIAPWRLPEF CERFQGRKDL LDYAQKHGIP VSATPKAPWS
     MDANIMHISY ESGILENPAK AAPEELYQMT QSVMKSSNTP IKVDITFKEG LPVTVLEHSG
     GKTLETPLEV LTFLNKIGGE QGVGRVDLVE NRFLGLKSRG VYETPGATIL HVAHKDMEVY
     CLDREIFRVK SFLALKMADY VYNGFWYSPE AEYVRTCLVG AQKNVSGKVT LEIFKGHVIA
     IARESTKTIY NQELASMDVH GTLSPYAATG FIEVNAMRLK EHYRVFGSAN ME
//