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Database: UniProt
Entry: Q03W70
LinkDB: Q03W70
Original site: Q03W70 
ID   ASSY_LEUMM              Reviewed;         408 AA.
AC   Q03W70;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   26-NOV-2014, entry version 58.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005};
DE            EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005};
GN   Name=argG {ECO:0000255|HAMAP-Rule:MF_00005};
GN   OrderedLocusNames=LEUM_1459;
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 /
OS   NCDO 523).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / NCDO 523;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC       diphosphate + N(omega)-(L-arginino)succinate. {ECO:0000255|HAMAP-
CC       Rule:MF_00005}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00005}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}.
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DR   EMBL; CP000414; ABJ62552.1; -; Genomic_DNA.
DR   RefSeq; WP_011680142.1; NC_008531.1.
DR   RefSeq; YP_818925.1; NC_008531.1.
DR   ProteinModelPortal; Q03W70; -.
DR   STRING; 203120.LEUM_1459; -.
DR   EnsemblBacteria; ABJ62552; ABJ62552; LEUM_1459.
DR   GeneID; 4423189; -.
DR   KEGG; lme:LEUM_1459; -.
DR   PATRIC; 22410901; VBILeuMes50664_1450.
DR   eggNOG; COG0137; -.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; APPEEAY; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   BioCyc; LMES203120:GJ8T-1459-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    408       Argininosuccinate synthase.
FT                                /FTId=PRO_0000321312.
FT   NP_BIND       8     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING      86     86       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     116    116       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING     118    118       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     122    122       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     122    122       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     123    123       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     126    126       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     174    174       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     259    259       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     271    271       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
SQ   SEQUENCE   408 AA;  44912 MW;  50269E18745D5E45 CRC64;
     MTDTLVLAYS GGLDTSVAIP WLKDKGYDVI AVVLDVGQHG KNLNEIQAKA LKVGAKQSIV
     IDAKAEFADK YVAPVIKANM MYEGEYPMVS ALSRPLIIKK LVDIAHENDA VAIAHGSTGH
     GNDQVRFEAA IHALDPDMKI EAPIRDFQWS REEEIQYAQE HDVPVPIDLD SPYSIDENLW
     GRANEAGILE NPWNQAPEDA FALTTAIEDA PDTPEFIDVT FEAGVPVALN GEVLSLEKLI
     VAVNEIAGKH GIGRIDHIEN RLVGIKSREI YEAPAAAVLM TAHKDLEDLT LERDVAHFKP
     IVEQQLANLV YEAKWVSPLF DSLMAFIDST QQNVNGVVKM KLFKGNATAV ARQSEHNSLY
     DEDLATYTSS SSFDQASAVG FIKLWTLSNT VYEQVNHVHS QAKKNTVK
//
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