AC   MF_00581;
DC   Protein; auto
TR   HAMAP; MF_00581; -; 1; level=0
XX
Names: Arg_succ_synth_type2
XX
ID   ASSY
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   Name=argG;
XX
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 2/3.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2
CC       subfamily.
XX
DR   Pfam; PF00764; Arginosuc_synth; 1; trigger=no
DR   NCBIfam; TIGR00032; ArgG; 1; trigger=no
DR   PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1; trigger=no
DR   PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Arginine biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
XX
GO   GO:0004055; F:argininosuccinate synthase activity
GO   GO:0005524; F:ATP binding
GO   GO:0006526; P:arginine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: ASSY_ECOLI (P0A6E4)
FT   BINDING         17..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: A
FT   BINDING         99
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: Y
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         131
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: T
FT   BINDING         135
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: N
FT   BINDING         135
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: N
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: D
FT   BINDING         136
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: D
FT   BINDING         139
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: R
FT   BINDING         192
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: S
FT   BINDING         194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: D
FT   BINDING         201
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: T
FT   BINDING         203
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: E
FT   BINDING         280
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT   Condition: E
XX
Size: 444-482;
Related: MF_00005;
Template: P0A6E4;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Argininosuccinate synthase type 1 subfamily in MF_00005.
XX
# Revision 1.40 2023/06/01
//