ID   ASTB_LEGPH              Reviewed;         448 AA.
AC   Q5ZUT4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=lpg1708;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
OS   ATCC 33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
RA   Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
RA   Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
RA   Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
RA   Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
RA   Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
RA   Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella
RT   pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU27788.1; -; Genomic_DNA.
DR   RefSeq; YP_095735.1; -.
DR   GeneID; 3078040; -.
DR   GenomeReviews; AE017354_GR; lpg1708.
DR   KEGG; lpn:lpg1708; -.
DR   NMPDR; fig|272624.3.peg.538; -.
DR   HOGENOM; Q5ZUT4; -.
DR   OMA; Q5ZUT4; HFAHHPA.
DR   BioCyc; LPNE272624:LPG1708-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_0000262357.
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    252    252       By similarity.
FT   ACT_SITE    372    372       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     216    216       Substrate (By similarity).
FT   BINDING     254    254       Substrate (By similarity).
FT   BINDING     366    366       Substrate (By similarity).
SQ   SEQUENCE   448 AA;  50134 MW;  C7B71B56141BE4E3 CRC64;
     MNVYELNMDG LVGQTHHYAG LSSGNIASTN NALSISNPQA AARQGLEKMR QLYNMGLKQG
     LLPPHQRPNL NLLYQLGFKG TPSEQINKAY KTAPELLSAC YSASSMWTAN AATVSASVDT
     EDNKVHFTAA NLISNLHRHQ EADFSKKLLE FIFSNSDYFN HHPLLPKSMG TSDEGAANHN
     RLCQSHAHSG INLFVYGKKV LGNHQFEQSP IKYPARQTKE ASEAIARNHL LNPERVIFAC
     QNPLAIDQGV FHNDVISVAN EHVFLVHEEA FYNQAYVLDQ LREKADFPLV IIQISKEQIS
     VSEAVDTYLF NSQLITLPDQ KNMILIAPAE CQANLKVKTC IDGLVADPQN PINSVYYLDL
     KQSMRNGGGP ACLRLRVPLN DYELKAMHQG ILIDNDLLDI LDKWVLKYYR TELKIPDLAD
     PQLLYECLDA LDELTQILKL GSIYPFQS
//