ID   ASSY_ALCBS              Reviewed;         407 AA.
AC   Q0VRM5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   Name=argG; OrderedLocusNames=ABO_0725;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL16173.1; -; Genomic_DNA.
DR   RefSeq; YP_692445.1; -.
DR   GeneID; 4213481; -.
DR   GenomeReviews; AM286690_GR; ABO_0725.
DR   KEGG; abo:ABO_0725; -.
DR   NMPDR; fig|393595.12.peg.728; -.
DR   HOGENOM; Q0VRM5; -.
DR   OMA; Q0VRM5; YVFPMFR.
DR   BioCyc; ABOR393595:ABO_0725-MON; -.
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.
FT                                /FTId=PRO_0000263904.
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     180    180       Citrulline (By similarity).
FT   BINDING     189    189       Citrulline (By similarity).
FT   BINDING     265    265       Citrulline (By similarity).
FT   BINDING     277    277       Citrulline (By similarity).
SQ   SEQUENCE   407 AA;  45442 MW;  EE3253CE29FDE9D6 CRC64;
     MSKINKVVLA YSGGLDTSVI VKWLQDTYDC EVVTFTADIG QGEEVEPARA KAEAMGVKEI
     YIEDLREEFV RDYVFPMFRA NAIYEGEYLL GTSIARPLIA KRLVEIAEET GADAISHGAT
     GKGNDQVRFE LGAYALAPGI QVIAPWREWD LNSREKLMAY CEERNIPVDF SNKKKKSPYS
     MDANLLHISY EGGNLEDPWW EAEEDMWRWS VSPEAAPDQA TYITLGFEKG DIVSIDGETL
     SPADVLTKLN KLGGDNGIGR LDIVENRYVG MKSRGCYETP GGTIMLPAHR AIESLTLDRE
     SAHLKDSVMP KYAELLYNGY WWSPERLALQ KLIDATQEHV NGEVRLKLYK GSVTVVGRRS
     DNDSLFDASI ATFEDDAGAY DQKDAEGFIK LNALRLRIAA KTGRKLS
//