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Database: UniProt
Entry: Q8KDE0
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Original site: Q8KDE0 
ID   ASSY_CHLTE              Reviewed;         401 AA.
AC   Q8KDE0;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   26-NOV-2014, entry version 79.
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}; OrderedLocusNames=CT1114;
OS   Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM72347.1; -; Genomic_DNA.
DR   RefSeq; NP_662005.1; NC_002932.3.
DR   RefSeq; WP_010932792.1; NC_002932.3.
DR   ProteinModelPortal; Q8KDE0; -.
DR   STRING; 194439.CT1114; -.
DR   EnsemblBacteria; AAM72347; AAM72347; CT1114.
DR   GeneID; 1006894; -.
DR   KEGG; cte:CT1114; -.
DR   PATRIC; 21400201; VBIChlTep116050_1012.
DR   eggNOG; COG0137; -.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; APPEEAY; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   BioCyc; CTEP194439:GHN0-1151-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.
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;
KW   Reference proteome.
FT   CHAIN         1    401       Argininosuccinate synthase.
FT                                /FTId=PRO_0000148583.
FT   NP_BIND       9     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING      88     88       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     118    118       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING     120    120       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     124    124       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     124    124       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     125    125       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     128    128       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     177    177       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     186    186       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     262    262       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     274    274       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
SQ   SEQUENCE   401 AA;  44423 MW;  4ECE7F2DEC336A6D CRC64;
     MSKEKIAVAY SGGLDTSVMI KWLKDKYEGA EIVAVTGNLG QKMEVDNLEQ KAIATGAKSF
     HFVDLRKTFV EEYIWKALKA GALYEDVYPL ATALGRPLLA KALVDVALAE GCTMLTHGCT
     GKGNDQVRFE VAFAALAPHM KVVAPLREWE FTSREQEIAY AMEHNIPVSA TKKNPYSIDE
     NIWGISIECG VLEDPMVAPP ADAYQITTAP ELAPDEPTVV DIEFAQGVPV ALDGQQMEGL
     DLIVRLNELG AMNGVGRLDM IENRVVGIKS REIYEAPAAT ILHFAHRELE RLTLEKSVFQ
     YKRNIGQDYA NLIYNGTWFS PMRKALDAFV DETQKPVTGM VRIKLYKGSM TLLGRTSPNS
     LYNEALATYT EADTFDHKSA EGFIKIYGLG LKTFHEVNKS E
//
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