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 01-MAY-2013, entry version 49.
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 OMA; IYNGYWW; -.
DR ProtClustDB; PRK00509; -.
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:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA: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 PANTHER; PTHR11587; PTHR11587; 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_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
//
