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Database: UniProt
Entry: Q0BVJ1
LinkDB: Q0BVJ1
Original site: Q0BVJ1 
ID   ASSY_GRABC              Reviewed;         416 AA.
AC   Q0BVJ1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   26-NOV-2014, entry version 56.
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=GbCGDNIH1_0263;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/JB.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K.,
RA   Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W.,
RA   Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61161.1; -; Genomic_DNA.
DR   RefSeq; YP_744084.1; NC_008343.1.
DR   ProteinModelPortal; Q0BVJ1; -.
DR   SMR; Q0BVJ1; 15-411.
DR   STRING; 391165.GbCGDNIH1_0263; -.
DR   EnsemblBacteria; ABI61161; ABI61161; GbCGDNIH1_0263.
DR   GeneID; 4274482; -.
DR   KEGG; gbe:GbCGDNIH1_0263; -.
DR   PATRIC; 22076553; VBIGraBet83793_0274.
DR   eggNOG; COG0137; -.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; APPEEAY; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   BioCyc; GBET391165:GHON-268-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    416       Argininosuccinate synthase.
FT                                /FTId=PRO_0000263930.
FT   NP_BIND      19     27       ATP. {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING      46     46       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING      97     97       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     102    102       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     127    127       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING     129    129       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     133    133       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     133    133       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     134    134       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     137    137       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     188    188       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     197    197       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     273    273       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     285    285       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
SQ   SEQUENCE   416 AA;  46235 MW;  23AAA2BA61B153C6 CRC64;
     MTRDIQTMAV KDVKKVVLAY SGGLDTSVIL RWLQTTYNCE VVTFTADLGQ GEELEPARRK
     AEMFGVKEIF VDDLRETFVK DFVFPMFRAN AVYEGQYLLG TSIARPLIAQ RQIEIAELTG
     ADAVAHGATG KGNDQVRFEL SYYALKPDVK VIAPWREWDL TSRTKLLEFA EANQIPIAKD
     KRGEAPFSVD ANLLHSSSEG KLLEDPAEEP DEIVYQRTIS PEAAPDKATI ITIDFEHGDP
     VAIDGIRLSP ATLLAKLNEL GKANGIGRLD LVENRFVGMK SRGVYETPGG TILLVAHRGI
     ESITLDREAA HLKDSLMPRY AELIYNGFWF SPERRMLQAA IDESQKSVTG RVRLKLYKGN
     TIVIGRESPN SLYSLKHVTF EDDQGAYDQV DAQGFIKLQS LRLRLAAIAG RRGGSL
//
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