ID   ASSY_BURCE     STANDARD;      PRT;   445 AA.
AC   P59608;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   16-MAY-2006, entry version 28.
DE   Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate
DE   ligase).
GN   Name=argG;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RX   MEDLINE=22638290; PubMed=12754231;
RX   DOI=10.1128/JB.185.11.3333-3343.2003;
RA   Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.;
RT   "Distribution and organization of auxotrophic genes on the
RT   multichromosomal genome of Burkholderia multivorans ATCC 17616.";
RL   J. Bacteriol. 185:3333-3343(2003).
CC   -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC       diphosphate + (N(omega)-L-arginino)succinate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       L-arginine from L-ornithine and carbamoyl phosphate: step 2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       2 subfamily.
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DR   EMBL; AB091438; BAC65286.1; -; Genomic_DNA.
DR   HSSP; P22767; 1KP3.
DR   SMR; P59608; 2-440.
DR   HAMAP; MF_00581; -; 1.
DR   InterPro; IPR001518; Arginosuc_synth.
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.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    445       Argininosuccinate synthase.
FT                                /FTId=PRO_0000148694.
FT   BINDING      17     17       ATP (By similarity).
FT   BINDING      43     43       ATP (By similarity).
FT   BINDING     129    129       ATP (By similarity).
FT   BINDING     131    131       ATP (By similarity).
FT   BINDING     136    136       ATP (By similarity).
FT   BINDING     194    194       ATP (By similarity).
FT   SITE         99     99       Citrulline binding (By similarity).
FT   SITE        131    131       Aspartate binding (By similarity).
FT   SITE        135    135       Citrulline and aspartate binding (By
FT                                similarity).
FT   SITE        136    136       Aspartate binding (By similarity).
FT   SITE        139    139       Citrulline binding (By similarity).
FT   SITE        192    192       Citrulline binding (By similarity).
FT   SITE        201    201       Citrulline binding (By similarity).
FT   SITE        203    203       Citrulline binding (By similarity).
FT   SITE        280    280       Citrulline binding (By similarity).
SQ   SEQUENCE   445 AA;  49252 MW;  67581060BC11267F CRC64;
     MSTILESLPT GQKVGIAFSG GLDTSAALHW MKLKGAVPYA YTANLGQPDE DDYDAIPKRA
     LEYGAAGARL IDCRAQLVAE GIAALQSGAF HITTAGVTYF NTTPIGRAVT GTMLVAAMKE
     DGVNIWGDGS TYKGNDIERF YRYGLLVNPD LKIYKPWLDQ TFIDELGGRA EMSEFMRQSG
     FAYKMSAEKA YSTDSNLLGA THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIAAEEVTVR
     FEAGQPVALN GVEFKDQVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL
     YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV
     KIELRRGNDY SILSTKSPNL TYQPERLSME KVASTFSPRD RIGQLTMRNL DITDTRDKLR
     VYTQVGLLTP GEASALPQIK GDSGE
//