ID   ASTE_BURXL              Reviewed;         342 AA.
AC   Q141D1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Succinylglutamate desuccinylase;
DE            EC=3.5.1.96;
GN   Name=astE; OrderedLocusNames=Bxeno_A1520; ORFNames=Bxe_A2918;
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: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate.
CC   -!- CATALYTIC ACTIVITY: N-succinyl-L-glutamate + H(2)O = succinate +
CC       L-glutamate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC   -!- SIMILARITY: Belongs to the aspA/astE family. Succinylglutamate
CC       desuccinylase subfamily.
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DR   EMBL; CP000270; ABE30058.1; -; Genomic_DNA.
DR   RefSeq; YP_558110.1; -.
DR   GeneID; 4004451; -.
DR   GenomeReviews; CP000270_GR; Bxeno_A1520.
DR   KEGG; bxe:Bxe_A2918; -.
DR   HOGENOM; Q141D1; -.
DR   OMA; Q141D1; EKFAIYP.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:HAMAP.
DR   GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP.
DR   HAMAP; MF_00767; -; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF017020; AstE; 1.
DR   TIGRFAMs; TIGR03242; arg_catab_astE; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Complete proteome; Hydrolase; Metal-binding;
KW   Zinc.
FT   CHAIN         1    342       Succinylglutamate desuccinylase.
FT                                /FTId=PRO_0000257710.
FT   ACT_SITE    222    222       Potential.
FT   METAL        63     63       Zinc (By similarity).
FT   METAL        66     66       Zinc (By similarity).
FT   METAL       159    159       Zinc (By similarity).
SQ   SEQUENCE   342 AA;  37411 MW;  FE230AF81640883E CRC64;
     MPVSLLDDFL AYTLAGTRPA ASEAQGTCAG GVRWSWLDDG VLLMEPAVQE EGMRSVLVSA
     GVHGDETAPI ELLAFLVRDI AHGTAALTGR LLVILGNVDA MRDACRYRDD DLNRLFSGRH
     LQLPQSHEAP RAAALERAAT RFFAAAPDNP GARWHIDMHT AIRASAFEQF ALLPHTGKPF
     SRAMFEWLGE ARISAVLLHT TRGNTYSHFT AQACGALACT LELGKVRPFG QNDLTRFAGA
     DHAVRHLLAG MRGEVRAPMP RAFTVIDQIT RQSEAFELLV APDVANFTPF AKDTVLARDG
     DYRYVVRHDE ERLVFPNATV KPGLRAGLMV IETTQDTLSK LV
//