ID   ASTE_BURCH              Reviewed;         342 AA.
AC   A0K610;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Succinylglutamate desuccinylase;
DE            EC=3.5.1.96;
GN   Name=astE; OrderedLocusNames=Bcen2424_1185;
OS   Burkholderia cenocepacia (strain HI2424).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA   Konstantinidis K., Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia
RT   HI2424.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate (By similarity).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000458; ABK07937.1; -; Genomic_DNA.
DR   RefSeq; YP_834830.1; -.
DR   GeneID; 4448253; -.
DR   GenomeReviews; CP000458_GR; Bcen2424_1185.
DR   KEGG; bch:Bcen2424_1185; -.
DR   HOGENOM; A0K610; -.
DR   OMA; A0K610; 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_1000017320.
FT   ACT_SITE    222    222       Potential.
FT   METAL        64     64       Zinc (By similarity).
FT   METAL        67     67       Zinc (By similarity).
FT   METAL       159    159       Zinc (By similarity).
SQ   SEQUENCE   342 AA;  36199 MW;  2508CEF510A9243A CRC64;
     MPAAALLDDF LAFTLAGDAP AERDGACAGG AVRWQWLGDG LLAFEPAATD AAARASVLVS
     AGVHGDETAP IELLSMLARD LVAGALPLAC RLLVVLGNVP AMRAGERYLD DDLNRLFSGR
     HAQVPASREA PRAAQLEAAA SAFFGAAPAG SARWHIDMHT AIRASVFEQF ALLPHTGTPP
     TRAMVEWLGD ARIAAVLLHT AKGNTYSHFT AEHCGALACT LELGKVRPFG QNDLTRFAPA
     DRAVRKLVSG GRAEGGATLP RVFTVIDQIT KQSDALELFV AADVANFTAF TRGTVLAQDG
     DYRYTVKHDE ERIVFPNPTV KPGLRAGLLV VDTTRDTLAA LV
//