ID   ASTB_CITK8              Reviewed;         447 AA.
AC   A8AHD7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-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=CKO_01771;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000822; ABV12900.1; -; Genomic_DNA.
DR   RefSeq; YP_001453336.1; -.
DR   GeneID; 5583623; -.
DR   GenomeReviews; CP000822_GR; CKO_01771.
DR   KEGG; cko:CKO_01771; -.
DR   OMA; A8AHD7; 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_1000065722.
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;  49250 MW;  F19A2DF42512AF16 CRC64;
     MKAHEVNFDG LVGLTHHYAG LSFGNEASIQ HRFQVSNPRL AAKQGLLKMK ALADAGFPQA
     VIPPHERPFI PVLRQLGFSG QDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATVCPSADA
     LDGKVHLTVA NLNNKFHRAL EAPTTASLLR AIFRDAQFFA VHDALPQVAL LGDEGAANHN
     RLGGDYGAPG IQLFVYGREE GVDTRPVRYP ARQTREASEA VARLNQVNPH QVIFARQNPD
     VIDLGVFHND VIAVSNRQVL FCHEQAFAKQ GELMRQLRSR VAGFMPLEVP AREVSVQDAV
     ATYLFNSQLL SRDDGSMVLV LPQECREHAG VWRYLNALLA ADNPISDLRV FDLRESMANG
     GGPACLRLRV VLTEDELRAV NPAVMMNDTL FSTLNDWVDR YYRDRLTAAD LADPQLLREG
     REALDTLTQL LNLGSVYPFQ QEGAGNG
//