(data stored in ACNUC7421 zone)

SWISSPROT: ASSY_PARDP

ID   ASSY_PARDP              Reviewed;         408 AA.
AC   A1AZB7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
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=Pden_0499;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC         arginino)succinate + AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472,
CC         ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; CP000489; ABL68611.1; -; Genomic_DNA.
DR   RefSeq; WP_011746844.1; NC_008686.1.
DR   SMR; A1AZB7; -.
DR   STRING; 318586.Pden_0499; -.
DR   PRIDE; A1AZB7; -.
DR   EnsemblBacteria; ABL68611; ABL68611; Pden_0499.
DR   KEGG; pde:Pden_0499; -.
DR   eggNOG; ENOG4105CDH; Bacteria.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; PAREWGM; -.
DR   BioCyc; PDEN318586:G1GW1-500-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01999; Argininosuccinate_Synthase; 1.
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;
DR   PRODOM; A1AZB7.
DR   SWISS-2DPAGE; A1AZB7.
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_0000321315.
FT   NP_BIND      11     19       ATP. {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING      38     38       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING      91     91       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING      96     96       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     121    121       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING     123    123       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     127    127       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     127    127       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     128    128       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     131    131       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     182    182       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     191    191       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     267    267       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     279    279       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
SQ   SEQUENCE   408 AA;  45468 MW;  3334B5E8EE303F82 CRC64;
     MSDAPKKVVL AYSGGLDTSI ILKWLQTEYG CEVITFTADL GQGEELEPAR QKAELLGIKP
     ENIHIVDVRE EFVRDFVFPM FRANAVYEGL YLLGTSIARP LISKHLVEIA HQHGADAVAH
     GATGKGNDQV RFELSAYALD PSIKVIAPWR EWDLTSRTKL IEFAEQNQIP IAKDKRGEAP
     FSVDANLLHT SSEGKALENP ADEAPDYVYQ RTVSPEDAPD QPEYIEVSFE RGDAVAINGE
     ALSPATILTA LNEYGRKHGI GRLDFVENRF VGMKSRGIYE TPGGTILLEA HRGIEQITLD
     SGAGHLKDSI MPRYAELIYN GFWYSPEREM LQALIDKSQE HVTGTVRLKL YKGGVHTVGR
     WSEHSLYSEK HVTFEDDAGA YDQKDAAGFI RLNALRLKLV ANRNARFK
//

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