ID   ASTB_SHEDO              Reviewed;         444 AA.
AC   Q12LR7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=Sden_2329;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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; CP000302; ABE55609.1; -; Genomic_DNA.
DR   RefSeq; YP_563332.1; -.
DR   GeneID; 4018822; -.
DR   GenomeReviews; CP000302_GR; Sden_2329.
DR   KEGG; sdn:Sden_2329; -.
DR   NMPDR; fig|318161.14.peg.2269; -.
DR   HOGENOM; Q12LR7; -.
DR   OMA; Q12LR7; KMKALME.
DR   BioCyc; SDEN318161:SDEN_2329-MON; -.
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    444       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_0000262374.
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    250    250       By similarity.
FT   ACT_SITE    368    368       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     214    214       Substrate (By similarity).
FT   BINDING     252    252       Substrate (By similarity).
FT   BINDING     362    362       Substrate (By similarity).
SQ   SEQUENCE   444 AA;  48882 MW;  1C234388F30C80A0 CRC64;
     MKHFEANFDG LVGPTHNYAG LSFGNVASYS NAAQTANPKA AAKQGLQKAK ALADLGMTQG
     VLAPQERPDL YTLRRIGFSG SDAEVIQKAA KQAPALLNAC CSASSMWTAN AATVSPSADT
     RDGKVHFTPA NLVDKLHRSI EPITTANILK ATFKDPHFFQ HHAHLPEHAH FGDEGAANHT
     RLCGEYGHSG VELFVYGQEA TNPNAPKPKK YPARQTLEAS QAIARLHQLE DESTVFMQQN
     PDVIDQGVFH NDVISVGNQN VLFYHEQAFL NTDAKFDEIR RKMNADMHFV KVATSQVSID
     DAVKSYLFNT QIITLPSGEM TIIAPTDCQE NLAVFAYLNE LVTLGTPIKQ VRYYDVKQSM
     QNGGGPACLR LRVALNDQEL AAVNQDTLMN DALFGRLNTW VEKHYRDSLS VKDLADPQLI
     VESRTALDEL TQILKLGSVY QFQK
//