ID   ASTB_PSEA6              Reviewed;         446 AA.
AC   Q15TB5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=Patl_2357;
OS   Pseudoalteromonas atlantica (strain T6c / BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-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; CP000388; ABG40873.1; -; Genomic_DNA.
DR   RefSeq; YP_661927.1; -.
DR   GeneID; 4172511; -.
DR   GenomeReviews; CP000388_GR; Patl_2357.
DR   KEGG; pat:Patl_2357; -.
DR   NMPDR; fig|342610.3.peg.1530; -.
DR   HOGENOM; Q15TB5; -.
DR   OMA; Q15TB5; HFAHHPA.
DR   BioCyc; PATL342610:PATL_2357-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    446       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_0000262363.
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    369    369       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     363    363       Substrate (By similarity).
SQ   SEQUENCE   446 AA;  49257 MW;  5070A42BD41CA902 CRC64;
     MKQFEVNFDG LVGPTHNYAG LSYGNVASLN NASAQSSPKQ AAKQGLKKMK ALADLGMIQG
     VLAPQARPDV DALRRLGFSG SDANVLQQAA KQAPAIFQAC CSASSMWTAN AATVSPSADT
     ADGKVHFTPA NLTNKYHRSL EPQVTGNILK ATFANQQYFS HHNHLPDNEH FGDEGAANHT
     RLCREYGERG VELFVYGRYA FDKSKPAPVK FPARQTFEAS QAVARLHGLS DDNVVFIQQN
     PDLIDQGVFH NDVISVGNQN VLFYHEQAFL DTDKAFAEIK QKYGAGDLHF IKVITEQVSL
     QDAIKSYLFN TQLVTLANGE MAIIAPTDCE ENPAVSAYLN ELVSLNTPIK HIRYYDVKQS
     MRNGGGPACL RLRVAMNETE LAAVNQSTMM NDAQFERLNN WVDKHYRDRL SVDDLRDVAL
     LNESRTALDE LTQLLKLGSV YPFQKV
//