(data stored in ACNUC7421 zone)

SWISSPROT: ASSY_EXIS2

ID   ASSY_EXIS2              Reviewed;         401 AA.
AC   B1YJ35;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 72.
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=Exig_0483;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) 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(+); Xref=Rhea:RHEA:10932,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00005};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 2/3. {ECO:0000255|HAMAP-
CC       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 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}.
DR   EMBL; CP001022; ACB59965.1; -; Genomic_DNA.
DR   RefSeq; WP_012369389.1; NC_010556.1.
DR   SMR; B1YJ35; -.
DR   STRING; 262543.Exig_0483; -.
DR   EnsemblBacteria; ACB59965; ACB59965; Exig_0483.
DR   KEGG; esi:Exig_0483; -.
DR   eggNOG; ENOG4105CDH; Bacteria.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; QCEVVTF; -.
DR   OrthoDB; 357142at2; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000001681; Chromosome.
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   SUPFAM; SSF69864; SSF69864; 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; B1YJ35.
DR   SWISS-2DPAGE; B1YJ35.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding.
FT   CHAIN           1..401
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_1000089036"
FT   NP_BIND         9..17
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         85
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         115
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         117
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         121
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         121
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         122
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         125
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         173
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         182
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         258
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         270
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   401 AA;  43512 MW;  68234CE4075548A1 CRC64;
     MTKQKLILAY SGGLDTSVAI KWLSKDYDVV ALCMDVGEGK DLSVIKEKAL LVGAIESIVL
     DVKDEFANDF VLPALQYGAH YEGAYPLISA LSRPLIAEKL VEVAHAQGAT AVAHGCTGKG
     NDQVRFEVSV AALDPSLEVI APVREWKWSR EEEIAYAKEN NVPIPINLNS PYSIDMNLWG
     RSNECGVLEN PWTEPPQDAY ALTVAPEDAP DQAEEVIIGF EAGVPVSING TAYPLAKLIT
     ELNIIAGAHG VGRIDHVENR LVGIKSREVY ECPGATVLLK AHAALETITL TKDVAHFKPI
     LSKQYAETIY NGLFHAPLTK GLKAFLTATQ QDVTGEVRVK LYKGNATVTG RQSAVSLYDE
     KLATYTKEDA FDHEAAKGFI KLHGLAISTH ASVHRQEGVK K
//

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