ID   ASTB_SALTY              Reviewed;         447 AA.
AC   Q8ZPU9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=STM1306;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   INDUCTION.
RX   MEDLINE=99173922; PubMed=10074092;
RA   Lu C.-D., Abdelal A.T.;
RT   "Role of ArgR in activation of the ast operon, encoding enzymes of the
RT   arginine succinyltransferase pathway in Salmonella typhimurium.";
RL   J. Bacteriol. 181:1934-1938(1999).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into
CC       N(2)-succinylornithine, ammonia and CO(2) (By similarity).
CC   -!- CATALYTIC ACTIVITY: N(2)-succinyl-L-arginine + 2 H(2)O = N(2)-
CC       succinyl-L-ornithine + 2 NH(3) + CO(2).
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 (By similarity).
CC   -!- INDUCTION: By nitrogen and carbon starvation, and arginine, via
CC       the argR and crp transcriptional regulators.
CC   -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
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DR   EMBL; AE008756; AAL20231.1; -; Genomic_DNA.
DR   RefSeq; NP_460272.1; -.
DR   SMR; Q8ZPU9; 3-441.
DR   GeneID; 1252824; -.
DR   GenomeReviews; AE006468_GR; STM1306.
DR   KEGG; stm:STM1306; -.
DR   NMPDR; fig|99287.1.peg.1264; -.
DR   HOGENOM; Q8ZPU9; -.
DR   OMA; Q8ZPU9; HFAHHPA.
DR   BioCyc; STYP99287:STM1306-MON; -.
DR   BRENDA; 3.5.3.23; 2.
DR   GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:HAMAP.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP.
DR   HAMAP; MF_01172; -; 1.
DR   InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB.
DR   Gene3D; G3DSA:3.75.10.20; SuccinylArg_di_hydro; 1.
DR   Pfam; PF04996; AstB; 1.
DR   TIGRFAMs; TIGR03241; arg_catab_astB; 1.
PE   2: Evidence at transcript level;
KW   Arginine metabolism; Complete proteome; Hydrolase.
FT   CHAIN         1    447       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_0000262373.
FT   REGION       19     28       Substrate binding (By similarity).
FT   REGION      137    138       Substrate binding (By similarity).
FT   ACT_SITE    174    174       By similarity.
FT   ACT_SITE    248    248       By similarity.
FT   ACT_SITE    365    365       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     212    212       Substrate (By similarity).
FT   BINDING     250    250       Substrate (By similarity).
FT   BINDING     359    359       Substrate (By similarity).
SQ   SEQUENCE   447 AA;  49192 MW;  B1C7296EBD1D7C9C 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
     ATYLFNSQLL SRNDGLMLLV LPRECQDHVG VWRYLNKLVA EDNPISAMQV FDLRESMANG
     GGPACLRLRV VLTEEERRAV NPAVMMNDAL FTALNAWADR YYRDRLTAAD LADPLLLREG
     REALDVLTRL LDLGSVYPFQ QTGAADG
//