ID   ASSY_ALHEH              Reviewed;         402 AA.
AC   Q0AB32;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   Name=argG; OrderedLocusNames=Mlg_0601;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily.
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DR   EMBL; CP000453; ABI55955.1; -; Genomic_DNA.
DR   RefSeq; YP_741445.1; -.
DR   GeneID; 4268480; -.
DR   GenomeReviews; CP000453_GR; Mlg_0601.
DR   KEGG; aeh:Mlg_0601; -.
DR   NMPDR; fig|187272.6.peg.574; -.
DR   HOGENOM; Q0AB32; -.
DR   OMA; Q0AB32; YVFPMFR.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00005; -; 1.
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;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    402       Argininosuccinate synthase.
FT                                /FTId=PRO_0000263905.
FT   NP_BIND      10     18       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      93     93       Citrulline (By similarity).
FT   BINDING     118    118       ATP; via amide nitrogen (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     179    179       Citrulline (By similarity).
FT   BINDING     188    188       Citrulline (By similarity).
FT   BINDING     264    264       Citrulline (By similarity).
FT   BINDING     276    276       Citrulline (By similarity).
SQ   SEQUENCE   402 AA;  45218 MW;  BDD7832EAAC6B57B CRC64;
     MSDVKKVVLA YSGGLDTSVI LQWLRETYDC EVVTFTADLG QGEELEPARK KAEAFGIKEI
     YIDDLREEFV RDFVFPMFRA NAIYEGEYLL GTSIARPLIA KRQVEIARET GADAVSHGAT
     GKGNDQVRFE LGYYGLEPNI KVIAPWREWD LNSREKLLAY AEKHGISIEG KQSGGSPYSM
     DANLLHISYE GGVLEDTWTE CEEAMWRWTR SPEAAPDEAQ YIDIEFQGGD PVSIDGEKLS
     PAALLSRLND LGAMHGVGRI DIVENRYVGM KSRGCYETPG GTILLRAHRA IESITLDRES
     AHLKDEVMPK YAELIYNGYW WSPEREAMQA LIDATQRRVN GVVRLKLYKG NVIVVGRDSA
     NDSLFDQTIA TFEDDRGAYD QKDAEGFIRL NALRLRIAQR RG
//