GenomeNet

Database: UniProt/SWISS-PROT
Entry: DAPE_PARL1
LinkDB: DAPE_PARL1
Original site: DAPE_PARL1 
ID   DAPE_PARL1              Reviewed;         395 AA.
AC   A7HPQ6;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   01-MAY-2013, entry version 41.
DE   RecName: Full=Succinyl-diaminopimelate desuccinylase;
DE            Short=SDAP desuccinylase;
DE            EC=3.5.1.18;
DE   AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase;
GN   Name=dapE; OrderedLocusNames=Plav_0266;
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Parvibaculum.
OX   NCBI_TaxID=402881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete genome sequence and annotation of Parvibaculum
RT   lavamentivorans DS-1.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-
CC       diaminopimelic acid (SDAP), forming succinate and LL-2,6-
CC       diaminoheptanedioate (DAP), an intermediate involved in the
CC       bacterial biosynthesis of lysine and meso-diaminopimelic acid, an
CC       essential component of bacterial cell walls (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O
CC       = succinate + LL-2,6-diaminoheptanedioate.
CC   -!- COFACTOR: Binds 1 Zn(2+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 Co(2+) ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 3/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. DapE 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; CP000774; ABS61889.1; -; Genomic_DNA.
DR   RefSeq; YP_001411546.1; NC_009719.1.
DR   ProteinModelPortal; A7HPQ6; -.
DR   STRING; 402881.Plav_0266; -.
DR   EnsemblBacteria; ABS61889; ABS61889; Plav_0266.
DR   GeneID; 5454257; -.
DR   KEGG; pla:Plav_0266; -.
DR   PATRIC; 22862062; VBIParLav90819_0279.
DR   eggNOG; COG0624; -.
DR   HOGENOM; HOG000243770; -.
DR   KO; K01439; -.
DR   OMA; WDAPRLE; -.
DR   ProtClustDB; PRK13009; -.
DR   BioCyc; PLAV402881:GHQA-316-MONOMER; -.
DR   UniPathway; UPA00034; UER00021.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:HAMAP.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_01690; DapE; 1; -.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR005941; DapE_proteobac.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Peptidase_M20_dimer; 1.
DR   TIGRFAMs; TIGR01246; dapE_proteo; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; FALSE_NEG.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cobalt; Complete proteome;
KW   Diaminopimelate biosynthesis; Hydrolase; Lysine biosynthesis;
KW   Metal-binding; Zinc.
FT   CHAIN         1    395       Succinyl-diaminopimelate desuccinylase.
FT                                /FTId=PRO_0000375640.
FT   ACT_SITE     83     83       By similarity.
FT   ACT_SITE    146    146       Proton acceptor (By similarity).
FT   METAL        81     81       Cobalt or zinc 1 (By similarity).
FT   METAL       114    114       Cobalt or zinc 1 (By similarity).
FT   METAL       114    114       Cobalt or zinc 2 (By similarity).
FT   METAL       147    147       Cobalt or zinc 2 (By similarity).
FT   METAL       175    175       Cobalt or zinc 1 (By similarity).
FT   METAL       364    364       Cobalt or zinc 2 (By similarity).
SQ   SEQUENCE   395 AA;  42041 MW;  4797D7D944CD5EC0 CRC64;
     MTAPASSPAS PYDPLDIAVE LIRCPSVTPD EGGALGVLEK WLAPLGFKCE RMRFSAEGTP
     DVDNLYARLG SGHPHFCFAG HTDVVPVGQA DAWSVDPFAA DIKDGRLYGR GAADMKSAVA
     SFVAAAERIS REGFQGSISL LITGDEEGPS INGTRKMLEK LAARNETIDH CIVGEPTSVE
     KLGDMIKVGR RGSINGWLTV QGTQGHVAYP HLADNPVPRL LEMLRRLDAH VLDEGTDHFQ
     PSNLEVTTVD IGNTATNVIP GSARATVNIR FNDLHTGASL DKWMRGVLDA VTAEMGGSYS
     FKTSVSGEAF ITEPGAFSAL IAEAAKEVTG ITPELSTTGG TSDARFIRAY APVVEIGLPN
     ATMHKADENT GVSEIRQLAD IYETVLRGYF AGRAS
//
DBGET integrated database retrieval system