ID   ASTB_SALPK              Reviewed;         447 AA.
AC   B5BA69;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=SSPA1429;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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}.
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DR   EMBL; FM200053; CAR59608.1; -; Genomic_DNA.
DR   RefSeq; WP_000123946.1; NC_011147.1.
DR   AlphaFoldDB; B5BA69; -.
DR   SMR; B5BA69; -.
DR   KEGG; sek:SSPA1429; -.
DR   HOGENOM; CLU_053835_0_0_6; -.
DR   OMA; TLNDWVD; -.
DR   UniPathway; UPA00185; UER00280.
DR   Proteomes; UP000001869; 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.
FT   CHAIN           1..447
FT                   /note="N-succinylarginine dihydrolase"
FT                   /id="PRO_1000138027"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   ACT_SITE        365
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         19..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         137..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ   SEQUENCE   447 AA;  49135 MW;  3E3AA7E7FC6DE4FD CRC64;
     MTAHEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AVKQGLLKMK ALADAGFPQA
     VIPPHERPFI PALRQLGFTG SDEQILDKVA RQAPRWLSSV SSASPMWVAN AATVCPSADA
     LDGKVHLTVA NLNNKFHRAL EAPVTEALLR AIFRDESQFS VHSALPQVAL LGDEGAANHN
     RLGGEYGSAG VQLFVYGREE ENEIRPARYP ARQSREASEA VARLNQVNPQ QVIFAQQNPE
     VIDQGVFHND VIAVSNRQVL FCHEAAFARQ KVLINQLRTR VDGFMAIEVP AGEVSVSDAV
     APYLFNSQLL SRDDGSMLLV LPRECQDHAG VWRYLNKLVA EDNPISAMQV FDLRESMANG
     GGPACLRLRV VLTEEERRAV NPAVMMNDAL FTALNAWADR YYRDRLTAAD LADPLLLREG
     REALDVLTRL LDLGSVYPFQ QTGAADG