ID   ASTB_ENTS8              Reviewed;         441 AA.
AC   A7MNV7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 9.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=ESA_02154;
OS   Enterobacter sakazakii (strain ATCC BAA-894).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000783; ABU77403.1; -; Genomic_DNA.
DR   RefSeq; YP_001438239.1; -.
DR   GeneID; 5549903; -.
DR   GenomeReviews; CP000783_GR; ESA_02154.
DR   KEGG; esa:ESA_02154; -.
DR   OMA; A7MNV7; 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    441       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_1000065727.
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   441 AA;  48522 MW;  E422303B74FD8446 CRC64;
     MKAREVNFDG LVGLTHHYAG LSFGNEASTK HRFQVSNPKL AARQGLAKMK ALADAGFPQA
     VIPPQERPNL AALRQIGFTG SDQQVLEKAW RAAPHLLSAA SSASSMWVAN AATVCPSADA
     LDGKVHLTVA NLNNKFHRAS EAPGTERLLR AIFRDESRFA VHGALPQVAM FGDEGAANHN
     RLGGDYGEPG LQLFIYGREE SGALVPARYP ARQTLEASQA VARLNQVDPQ RVMFAQQNPA
     VIDQGVFHND VIAVSNRQVL FCHEHAFLHQ QALFDALAEK VPGFTPLVVP AGAVSVQDAV
     ETYLFNSQLL SRDDGTMVLV LPEESRRHEG VWRYLNTLVA ADNPISELKV FDLRESMANG
     GGPACLRLRV VLTDDERQAV NPAVMMDDTL FTRLNAWVDK YYRDRLTQED LVDPQLLREG
     REALDELSRL LSLGNVYPFQ Q
//