ID   ASSY_ANOGA              Reviewed;         424 AA.
AC   Q7PR38;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 128.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   ORFNames=AGAP003015;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-citrulline + L-aspartate + ATP = 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   -!- 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; AAAB01008859; EAA07894.4; -; Genomic_DNA.
DR   AlphaFoldDB; Q7PR38; -.
DR   SMR; Q7PR38; -.
DR   FunCoup; Q7PR38; 663.
DR   STRING; 7165.Q7PR38; -.
DR   PaxDb; 7165-Q7PR38; -.
DR   EnsemblMetazoa; AGAMI1_003975.R6879; AGAMI1_003975.P6879; AGAMI1_003975.
DR   EnsemblMetazoa; AGAP003015-RA; AGAP003015-PA; AGAP003015.
DR   GeneID; 1272938; -.
DR   KEGG; aga:1272938; -.
DR   CTD; 40812; -.
DR   VEuPathDB; VectorBase:AGAMI1_003975; -.
DR   VEuPathDB; VectorBase:AGAP003015; -.
DR   eggNOG; KOG1706; Eukaryota.
DR   HOGENOM; CLU_032784_4_2_1; -.
DR   InParanoid; Q7PR38; -.
DR   OMA; WRWTVSP; -.
DR   OrthoDB; 1688907at2759; -.
DR   PhylomeDB; Q7PR38; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000007062; Chromosome 2R.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; IBA:GO_Central.
DR   CDD; cd01999; ASS; 1.
DR   FunFam; 3.40.50.620:FF:000019; Argininosuccinate synthase; 1.
DR   FunFam; 3.90.1260.10:FF:000003; Argininosuccinate synthase; 1.
DR   Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR   InterPro; IPR048268; Arginosuc_syn_C.
DR   InterPro; IPR048267; Arginosuc_syn_N.
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   NCBIfam; TIGR00032; argG; 1.
DR   NCBIfam; NF001770; PRK00509.1; 1.
DR   PANTHER; PTHR11587; ARGININOSUCCINATE SYNTHASE; 1.
DR   PANTHER; PTHR11587:SF2; ARGININOSUCCINATE SYNTHASE; 1.
DR   Pfam; PF20979; Arginosuc_syn_C; 1.
DR   Pfam; PF00764; Arginosuc_synth; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 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; Cytoplasm;
KW   Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..424
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_0000321327"
FT   BINDING         9..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
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"
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   424 AA;  47807 MW;  133485FD4A9CC4B3 CRC64;
     MSKEKVLLAY SGGLDTSCIL KWLLEQDYEV ICFMADVGQT EDFAAAREKA LKIGAADVVV
     KDMKDFFVEK FVWPAVQMGL IYEDRYLLGT SLARPCISKG LMDVAVQRGC SYISHGATGK
     GNDQIRFELS CYALSPTIRV IAPWRMETFC QRFQGRSDLL EYAKRSNIPV SATTKAPWSM
     DANIMHISYE SGILEDPSVA APEELYQLTQ SPTRAPDTPT VAEIVFKAGL PVRVTELVSG
     RTMERPVDIL AFLNKAGGEH GVGRIDIVEN RYIGLKSRGV YETPGVTVLH CAHRDLEIYC
     LDREVLRVKK YLADRMADYV YNGYWYAPEA EYVRKCILES QKHVSGKVVV EMFKGHVMVT
     SRESMHSLYN QELASMEVHG NFSPYSSTGF IEINAVRLRE HHRVFGTANM TKHFSRTESD
     MKLI
//