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Database: UniProt
Entry: Q1GCK1
LinkDB: Q1GCK1
Original site: Q1GCK1 
ID   ASSY_RUEST              Reviewed;         407 AA.
AC   Q1GCK1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   14-MAY-2014, entry version 53.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   Name=argG; OrderedLocusNames=TM1040_2883;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
RG   US DOE Joint Genome Institute;
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., Brettin T., Bruce D., Han C., Tapia R., Goodwin L.,
RA   Thompson L.S., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M.,
RA   Schell M.A., Sun F., Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-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 (By similarity).
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily.
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DR   EMBL; CP000377; ABF65615.1; -; Genomic_DNA.
DR   RefSeq; YP_614877.1; NC_008044.1.
DR   ProteinModelPortal; Q1GCK1; -.
DR   SMR; Q1GCK1; 6-404.
DR   STRING; 292414.TM1040_2883; -.
DR   EnsemblBacteria; ABF65615; ABF65615; TM1040_2883.
DR   GeneID; 4076417; -.
DR   KEGG; sit:TM1040_2883; -.
DR   PATRIC; 23390068; VBIRueSp69653_3833.
DR   eggNOG; COG0137; -.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   BioCyc; RSP292414:GHCT-2934-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.1260.10; -; 1.
DR   HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR   InterPro; IPR001518; Arginosuc_synth.
DR   InterPro; IPR018223; Arginosuc_synth_CS.
DR   InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
DR   InterPro; IPR024074; AS_cat/multimer_dom_body.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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_0000263973.
FT   NP_BIND      10     18       ATP (By similarity).
FT   BINDING      37     37       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING      90     90       Citrulline (By similarity).
FT   BINDING      95     95       Citrulline (By similarity).
FT   BINDING     120    120       ATP; via amide nitrogen (By similarity).
FT   BINDING     122    122       Aspartate (By similarity).
FT   BINDING     126    126       Aspartate (By similarity).
FT   BINDING     126    126       Citrulline (By similarity).
FT   BINDING     127    127       Aspartate (By similarity).
FT   BINDING     130    130       Citrulline (By similarity).
FT   BINDING     181    181       Citrulline (By similarity).
FT   BINDING     190    190       Citrulline (By similarity).
FT   BINDING     266    266       Citrulline (By similarity).
FT   BINDING     278    278       Citrulline (By similarity).
SQ   SEQUENCE   407 AA;  45385 MW;  63F18DC0CF23A370 CRC64;
     MSAPKKVVLA YSGGLDTSII LKWLQTEYGC EVVTFTADLG QGEELEPARK KAELLGIKPE
     NIFIEDIREE FVRDFVFPMF RANAVYEGLY LLGTSIARPL ISKRLVEIAE ATGADAVSHG
     ATGKGNDQVR FELSAYALNP DIKVIAPWRE WDLTSRTKLL EFAEANQIPI AKDKRGEAPF
     SVDANLLHTS SEGKVLEDPA EMAPDYVYQR TVNPEDAPNE PEFIEITFEK GDAVAINGEA
     MSPATILTKL NEYGRKHGIG RLDFVENRFV GMKSRGIYEA PGGDILLEAH RGIEQITLDS
     GAGHLKDSIM PRYAELIYNG FWYSPEREML QALIDESQKH VTGTVRVKLY KGSAKTVGRW
     SEHSLYSEAH VTFEEDAGAY DQKDAQGFIQ LNALRLKLLA ARNRRVK
//
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