ID   ASTB_BURXL              Reviewed;         446 AA.
AC   Q141D2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=Bxeno_A1519; ORFNames=Bxe_A2919;
OS   Burkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE30057.1; -; Genomic_DNA.
DR   RefSeq; YP_558109.1; -.
DR   GeneID; 4004450; -.
DR   GenomeReviews; CP000270_GR; Bxeno_A1519.
DR   KEGG; bxe:Bxe_A2919; -.
DR   HOGENOM; Q141D2; -.
DR   OMA; Q141D2; 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   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_0000262344.
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    249    249       By similarity.
FT   ACT_SITE    370    370       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     213    213       Substrate (By similarity).
FT   BINDING     251    251       Substrate (By similarity).
FT   BINDING     364    364       Substrate (By similarity).
SQ   SEQUENCE   446 AA;  48896 MW;  3FF0ECB529441E9A CRC64;
     MQATEANFDG LVGPTHNYAG LSFGNVASQN NEKSVANPKA AAKQGLRKMK QLADLGFHQG
     VLPPQERPSM RLLRELGFSG DDATVIARVA RDAPELLAAA SSASAMWTAN AATVSPSADT
     NDGRVHFTPA NLCSKLHRAI EHESTRRTLR TMFNDTDRFV VHEALPGTPA LGDEGAANHT
     RFCEEYGARG VEFFVYGRSE YRRGPEPKRF PARQSFEASR AVAHRHGLAD EATVYAQQNP
     DVIDAGVFHN DVIAVGNRNT LFCHQFAFVE PNAVYDELRA KLSGLKAAFN VIEVPDAQVS
     VADAVSSYLF NSQLLTRPDG KQVLVVPQEC RENPRVAAYL DDLTSRTGPI DDVLVFDLRE
     SMKNGGGPAC LRLRVVLDDA ERAAVTPGVW IDDTLFGRLD AWIEKHYRDR LAPADLTDPH
     LLAESRTALD ELTQILGLGS LYDFQR
//