ID   ASTB_YERE8              Reviewed;         447 AA.
AC   A1JS35;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=YE2466;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the
RT   high pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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   -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
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DR   EMBL; AM286415; CAL12509.1; -; Genomic_DNA.
DR   RefSeq; YP_001006673.1; -.
DR   GeneID; 4712504; -.
DR   GenomeReviews; AM286415_GR; YE2466.
DR   KEGG; yen:YE2466; -.
DR   NMPDR; fig|630.2.peg.2389; -.
DR   OMA; A1JS35; HFAHHPA.
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   3: Inferred from homology;
KW   Arginine metabolism; Complete proteome; Hydrolase.
FT   CHAIN         1    447       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_1000065742.
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    249    249       By similarity.
FT   ACT_SITE    370    370       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     213    213       Substrate (By similarity).
FT   BINDING     251    251       Substrate (By similarity).
FT   BINDING     364    364       Substrate (By similarity).
SQ   SEQUENCE   447 AA;  49368 MW;  99C6026B739549C0 CRC64;
     MAGYEVNFDG LVGLTHHYAG LSFGNEASTR HQNTLSNPRL AAKQGLLKMK ALADLGYKQG
     VLPPQERPAM GVLRQLGFSG SDEQVLSEVV RKSPRLLSAV SSASSMWTAN AATVSPAADS
     ADGRVHFTVA NLNNKFHRAI EADTTSAILK SIFNNHRHFV HHDALPSVEL FGDEGAANHN
     RLGGEYDRPA IQVFVYGRQG FEGGAMPSRY PARQTLEASE AVARLHLLDP ERAVFVQQNP
     AVIDQGVFHN DVIAVSNQNV LFHHQHAFVP DIRVMEDLRR KMGRIEQQLF TIEVPAAQVS
     VAQAVSSYLF NSQLLSKANG KMLLVIPQES QECPAVWEYL SELINSGGPI DEVRVFDLRE
     SMHNGGGPAC LRLRVALNDT ELAAVNSRVM MTPALFVALN NWVDQHYRDR LQFKDLADPQ
     LLQEGRQALD ELTKILNLGS IYPFQHL
//