ID   ASSY1_RHIL3             Reviewed;         403 AA.
AC   Q1MEZ8;
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 1;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase 1;
GN   Name=argG1; OrderedLocusNames=RL2987;
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.
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DR   EMBL; AM236080; CAK08476.1; -; Genomic_DNA.
DR   RefSeq; YP_768571.1; -.
DR   GeneID; 4400740; -.
DR   GenomeReviews; AM236080_GR; RL2987.
DR   KEGG; rle:RL2987; -.
DR   NMPDR; fig|216596.1.peg.3091; -.
DR   HOGENOM; Q1MEZ8; -.
DR   OMA; Q1MEZ8; WAARNGR.
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    403       Argininosuccinate synthase 1.
FT                                /FTId=PRO_0000263961.
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   403 AA;  44319 MW;  4A143B783BBD0634 CRC64;
     MTKIEKIVLS YSGGLDTSII LKWLQETYGC EVVTFTADLG QGEELEPARA KAEMSGVKDI
     RIVDLREEFV SDFVFPMLRA NALYEGQYLL GSSIARPLIA KHLVGIAREV GADAVAHGAT
     GKGNDQIRFE LAVNALDPSI KVIAPWRQWN IRSRLQLSEY AEKHRIPVPS DKRGEAPFSI
     DANLLHTSTE GKSLENPAEV APDHVYQRTV DPVDAPDTPE IITVGFERGD PVSVNGKAMT
     PAALLTELNG LGGRHGVGRL DLVENRFIGM KSRGIYETPG GTILLAAHRG IESITLDRAA
     AHLKDEIMPR YAELIYNGFW FAPEREMLQA LIDHSQAFVS GEVTLRLYKG SASVISRASP
     CSLYSADLVT FEESTIAFDH HDAEGFIRLN GLRLRSWAAR NGR
//