ID   ASSY2_RHIL3             Reviewed;         407 AA.
AC   Q1MAN9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Argininosuccinate synthase 2;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase 2;
GN   Name=argG2; OrderedLocusNames=RL4515;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R.,
RA   Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D.,
RA   Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C.,
RA   Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A.,
RA   Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and
RT   accessory components.";
RL   Genome Biol. 7:RESEARCH34.1-RESEARCH34.20(2006).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM236080; CAK09999.1; -; Genomic_DNA.
DR   RefSeq; YP_770080.1; -.
DR   GeneID; 4400741; -.
DR   GenomeReviews; AM236080_GR; RL4515.
DR   KEGG; rle:RL4515; -.
DR   NMPDR; fig|216596.1.peg.4648; -.
DR   HOGENOM; Q1MAN9; -.
DR   OMA; Q1MAN9; 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    407       Argininosuccinate synthase 2.
FT                                /FTId=PRO_0000263962.
FT   NP_BIND      13     21       ATP (By similarity).
FT   BINDING      40     40       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING      91     91       Citrulline (By similarity).
FT   BINDING      96     96       Citrulline (By similarity).
FT   BINDING     121    121       ATP; via amide nitrogen (By similarity).
FT   BINDING     123    123       Aspartate (By similarity).
FT   BINDING     127    127       Aspartate (By similarity).
FT   BINDING     127    127       Citrulline (By similarity).
FT   BINDING     128    128       Aspartate (By similarity).
FT   BINDING     131    131       Citrulline (By similarity).
FT   BINDING     182    182       Citrulline (By similarity).
FT   BINDING     191    191       Citrulline (By similarity).
FT   BINDING     267    267       Citrulline (By similarity).
FT   BINDING     279    279       Citrulline (By similarity).
SQ   SEQUENCE   407 AA;  45177 MW;  FD48DFBDB2D285DD CRC64;
     MASYKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP ARKKAEMLGI
     KEIYIEDVRE EFVRDFVFPM FRANAVYEGV YLLGTSIARP LISKHLIDIA KKTGADAIAH
     GATGKGNDQV RFELSAYALN PDIKIIAPWR DWAFKSRTDL LAFAEQHQIP VAKDKMGEAP
     FSVDANLLHS SSEGKVLEDP SQEAPEYVHM RTISPEAAPD KATTIKVGFE KGDAVSINGV
     RMSPATLLAA LNNYGRDNGI GRLDLVENRF VGMKSRGVYE TPGGTILLTA HRAIESITLD
     RGAAHLKDDI MPRYAELIYY GFWFSPEREM LQALIDKSQE HVEGEVTLKL YKGNVMVIGR
     ESDKSLYSDK LVTFEDDQGA YDQKDAAGFI KLNALRLRTL AKRNLVK
//