ID   ASTB_PSEPF              Reviewed;         448 AA.
AC   Q3K886;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=Pfl01_4281;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyripides N., Anderson I., Richardson P.;
RT   "Complete sequence of Pseudomonas fluorescens PfO-1.";
RL   Submitted (AUG-2005) 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; CP000094; ABA76018.1; -; Genomic_DNA.
DR   RefSeq; YP_350009.1; -.
DR   GeneID; 3712893; -.
DR   GenomeReviews; CP000094_GR; Pfl01_4281.
DR   KEGG; pfo:Pfl01_4281; -.
DR   HOGENOM; Q3K886; -.
DR   OMA; Q3K886; KMKALME.
DR   BioCyc; PFLU205922:PFL_4281-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    448       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_0000262366.
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;  48728 MW;  66F70560E487848A CRC64;
     MKSYEVNFDG LVGPTHNYGG LSYGNVASQS NSQQSSNPKE AALQGLAKMK ALMEMGFQQG
     VLAPQERPDV AALRRLGFSG TDAQVIERAA KEAMPLLVAS CSASSMWVAN AATVSPSADT
     ADGRVHFTAA NLNCKYHRSI EHPTTSRVLG AMFANQQHFA HHAALPAVAQ FGDEGAANHT
     RFCREYGDAG VEFFVFGRSA FDTRYPAPQK YPARQTLEAS QAVARLHGLR DDGVVYAQQN
     PAVIDQGVFH NDVIAVGNGE VLFYHEDAFL DTDQMLAELQ AKLAKVGGKF QSVCVPRSAV
     TVDDAVRSYL FNSQLLSRPD GSMLLIVPEE CRGNERVWNY LQGLTSSGGL IREVKVFDLK
     QSMQNGGGPA CLRLRVALNE TELAAVNPGV IMTAPLYGSL TAWVEKHYRD RLTESDLADP
     QLLLECRTAL DELTQILKLG AVYPFQIN
//