ID   ASTB_SHIDS              Reviewed;         448 AA.
AC   Q32G87;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=N-succinylarginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_01172};
DE            EC=3.5.3.23 {ECO:0000255|HAMAP-Rule:MF_01172};
GN   Name=astB {ECO:0000255|HAMAP-Rule:MF_01172}; OrderedLocusNames=SDY_1532;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC       succinylornithine, ammonia and CO(2). {ECO:0000255|HAMAP-
CC       Rule:MF_01172}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01172};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01172}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01172}.
CC   -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01172}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB61668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000034; ABB61668.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_403159.2; NC_007606.1.
DR   AlphaFoldDB; Q32G87; -.
DR   SMR; Q32G87; -.
DR   STRING; 300267.SDY_1532; -.
DR   EnsemblBacteria; ABB61668; ABB61668; SDY_1532.
DR   KEGG; sdy:SDY_1532; -.
DR   PATRIC; fig|300267.13.peg.1835; -.
DR   HOGENOM; CLU_053835_0_0_6; -.
DR   UniPathway; UPA00185; UER00280.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR   GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.75.10.20; -; 1.
DR   HAMAP; MF_01172; AstB; 1.
DR   InterPro; IPR037031; AstB_sf.
DR   InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB.
DR   Pfam; PF04996; AstB; 1.
DR   TIGRFAMs; TIGR03241; arg_catab_astB; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Hydrolase; Reference proteome.
FT   CHAIN           1..448
FT                   /note="N-succinylarginine dihydrolase"
FT                   /id="PRO_0000262378"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   ACT_SITE        366
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         20..29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         138..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ   SEQUENCE   448 AA;  49589 MW;  E16919C350C64521 CRC64;
     MRNAWEVNFD GLVGLTHNYA GLLFGNEAST RHRFQVSNPR LAAKQGLLKM KNLADAGFPQ
     AVIPPHERPF IPVLRQLGFS GSDEQVLEKV ARQAPHWLSS VSSASPMWVA NAATIAPSVD
     TLDGKVHRTV ANLNNKFHRS LEAPVTESLL KAIFNDEEKF SVHSALPQVA LLGDEGAANH
     NRLGGHYGEP GMQLFVYGRE KGNDTRPSRY PARQTREASE AVARLNQVNP QQVIFAQQNP
     DVIDQGVFHN DVIAVSNRQV LFCHQQAFAR QSQLLANLRA RVNGFMAIEV PATQVSVSDA
     VSTYLFNSQL LSRDDGSMML VLPQECREHA GVWCYLNELL AADNPISELK VFDLRESMAN
     GGGPACLRLR VVLTEEERRA VNPAVMMNDT LFNALNDWGD RYYRDRLTDA DLADPQLLRE
     GREALDVLSQ LLNLGSVYPF QREGGGNG