AC   MF_01172;
DC   Protein; auto
TR   HAMAP; MF_01172; -; 1; level=0
XX
Names: AstB
XX
ID   ASTB
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB;
XX
CC   -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC       succinylornithine, ammonia and CO(2).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-
CC         succinyl-L-ornithine + 2 NH4(+); Xref=Rhea:RHEA:19533,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58241, ChEBI:CHEBI:58514; EC=3.5.3.23;
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
XX
DR   Pfam; PF04996; AstB; 1; trigger=no
DR   NCBIfam; TIGR03241; arg_catab_astB; 1; trigger=no
XX
KW   Arginine metabolism
KW   Hydrolase
XX
GO   GO:0009015; F:N-succinylarginine dihydrolase activity
GO   GO:0019544; P:arginine catabolic process to glutamate
XX
FT   From: ASTB_ECOLI (P76216)
FT   BINDING         19..28
FT                   /ligand="substrate"
FT   BINDING         137..138
FT                   /ligand="substrate"
FT   ACT_SITE        174
FT   Condition: E
FT   ACT_SITE        248
FT   Condition: H
FT   ACT_SITE        365
FT                   /note="Nucleophile"
FT   Condition: C
FT   BINDING         110
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         212
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         250
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         359
FT                   /ligand="substrate"
FT   Condition: N
XX
Size: 415-449;
Related: None;
Template: P76216;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: in CAUVC
Plasmid: None
Comments: None
XX
# Revision 1.22 2023/06/01
//