ASSY_DICTD
ID ASSY_DICTD Reviewed; 397 AA.
AC B8E0N9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Dtur_1787;
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=515635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK43059.1; -; Genomic_DNA.
DR RefSeq; WP_012584133.1; NC_011661.1.
DR RefSeq; YP_002353673.1; NC_011661.1.
DR AlphaFoldDB; B8E0N9; -.
DR SMR; B8E0N9; -.
DR STRING; 515635.Dtur_1787; -.
DR EnsemblBacteria; ACK43059; ACK43059; Dtur_1787.
DR KEGG; dtu:Dtur_1787; -.
DR PATRIC; fig|515635.4.peg.1839; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_0; -.
DR InParanoid; B8E0N9; -.
DR OMA; QCEVVTF; -.
DR OrthoDB; 357142at2; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..397
FT /note="Argininosuccinate synthase"
FT /id="PRO_1000191893"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 87
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 119
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 124
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 127
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 175
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 184
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 257
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 269
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
SQ SEQUENCE 397 AA; 44986 MW; 2883E3E95625C03B CRC64;
MEREKVVLAY SGGLDTSVAI KWLMQKYSLD VITLTVDIGQ GIDLNEIKNK AENLGVEKAY
VLDLREEFIK DYIIPAIKSN AMYERVYPLA TALSRPLIAK YLVKVAKENG AKYVAHGCTG
KGNDQVRIDL GVKALAPDLE IIAPVREWNF SREEEIEYAI ENNIPIPVSR KNPYSIDENL
WGRSIEGGIL EDPWQEPPED IYLWTKLENK EPSYIEITFE KGIPVKLNGV EKDLVGLIEE
LNKIAGSYGI GRIDHIENRL VGIKSREIYE APAALVIIKA HEALEDLVLP RELAHFKRML
EDKYAELVYY GLWFDPFREA LQAFMDKTQE RVTGKVKIKL IPWSFSIVGR DSPYSLYDHS
LATYDKGSTF STESAVGFIK LFGLQNYLYA LKGGKNA
