ID   ASTB_PSEMY              Reviewed;         448 AA.
AC   A4XWE6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=Pmen_2907;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA   Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-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; CP000680; ABP85662.1; -; Genomic_DNA.
DR   RefSeq; YP_001188394.1; -.
DR   GeneID; 5107625; -.
DR   GenomeReviews; CP000680_GR; Pmen_2907.
DR   KEGG; pmy:Pmen_2907; -.
DR   OMA; A4XWE6; 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   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    448       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_1000065732.
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    371    371       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     365    365       Substrate (By similarity).
SQ   SEQUENCE   448 AA;  48693 MW;  FCF434B81E25F748 CRC64;
     MTAYEMNFDG LVGPTHNYGG LSYGNVASQS NSQAISNPKE AAKQGLAKMK ALMDMGFKQG
     VLAPQERPDV AALRRLGFTG SDPEVIARAA REAMPLLVAS CSASSMWTAN ACTVSPSADT
     ADARVHFTAA NLNCKFHRSI EHPTTSRVLQ AMFASQEHFA HHPALPAVSQ FGDEGAANHT
     RFCKSYGEPG VEFFVYGRSA FDSRYPAPAR YPARQTLEAS QAVARLHGLS EEGVVYAQQN
     PAVIDQGVFH NDVIAVGNGE VLFYHQDAFL DTDKVLGELG SKLAGRGGNF QAVCVPNSAV
     SVEDAVKSYL FNSQLLTRAD GSMLLVVPEE CRNNASVWRY LEQLTAGNGP IREVRVFDLK
     QSMQNGGGPA CLRLRVALKE QELAAVNPGV VMSLELHDRL VAWVDKHYRD RLSEADLADP
     QLLIECRTAL DELTQILKLG SVYPFQMT
//