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ASSY_DESRM
ID   ASSY_DESRM              Reviewed;         401 AA.
AC   A4J173;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Dred_0277;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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}.
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DR   EMBL; CP000612; ABO48826.1; -; Genomic_DNA.
DR   RefSeq; WP_011876664.1; NC_009253.1.
DR   AlphaFoldDB; A4J173; -.
DR   SMR; A4J173; -.
DR   STRING; 349161.Dred_0277; -.
DR   EnsemblBacteria; ABO48826; ABO48826; Dred_0277.
DR   KEGG; drm:Dred_0277; -.
DR   eggNOG; COG0137; Bacteria.
DR   HOGENOM; CLU_032784_4_2_9; -.
DR   OMA; QCEVVTF; -.
DR   OrthoDB; 357142at2; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000001556; 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;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..401
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_0000321310"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         85
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         90
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         117
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         121
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         121
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         122
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         125
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         174
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         183
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         259
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         271
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   401 AA;  44270 MW;  79BD041B2BDCFECE CRC64;
     MPKVVLAYSG GLDTSVIIAW LKENYGYEVI AVTADLGQGE ELAPLEEKAL QSGASKIYIE
     DLRKEFVEDY IWPTLKAGAI YEGKYLLGTS FARPLIAKKL VEIAEKEGAV AVAHGATGKG
     NDQVRFELGV KALAPHLKVI APWREWDIRS REDAIDYAEA RGIPVPVTKK SIYSRDRNIW
     HISHEGGELE SPANAASYDM LMLTVPPEKA PDQPTYVEIG FEKGIPVSIN GELMDSIGLL
     EKLNVIGGEN GIGIVDMVEN RLVGMKSRGV YETPGGAILV YAHRELELLT LDRATLHYKE
     QIALRYAELV YDGVWFAPLR EALDAFVDNT QRTVTGTVKL KLYKGNMMPA GVTSPYSLYD
     EELSTFGRDE VYNQADAAGF INLFGLPLKV RAMMEKKAGL R
 
 
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