ID   DAPEL_LISIV             Reviewed;         372 AA.
AC   Q6LAN3;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=N-acetyldiaminopimelate deacetylase {ECO:0000255|HAMAP-Rule:MF_01692};
DE            EC=3.5.1.47 {ECO:0000255|HAMAP-Rule:MF_01692};
OS   Listeria ivanovii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19119 / DSM 20750 / BCRC 14844 / JCM 7681 / KCTC 3444 / NCTC
RC   11846 / NRRL B-33017 / SLCC 2379 / WDCM 00018;
RA   Dominguez G.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC       diaminopimelate and acetate. {ECO:0000255|HAMAP-Rule:MF_01692}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-
CC         diaminoheptanedioate + acetate; Xref=Rhea:RHEA:20405,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:58767; EC=3.5.1.47; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01692};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (acetylase route): step 3/3. {ECO:0000255|HAMAP-Rule:MF_01692}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC       acetyldiaminopimelate deacetylase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01692}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X98994; CAC79603.1; -; Genomic_DNA.
DR   RefSeq; WP_014092435.1; NZ_PPPI01000001.1.
DR   AlphaFoldDB; Q6LAN3; -.
DR   SMR; Q6LAN3; -.
DR   MEROPS; M20.A27; -.
DR   GeneID; 57075942; -.
DR   OMA; RAHACGH; -.
DR   UniPathway; UPA00034; UER00024.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01692; DapEL; 1.
DR   InterPro; IPR023905; AcetylDAP_deacetylase.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR11014; PTHR11014; 1.
DR   PANTHER; PTHR11014:SF98; PTHR11014:SF98; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis.
FT   CHAIN           1..372
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000376772"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ   SEQUENCE   372 AA;  41470 MW;  E8147EE5E1581CAC CRC64;
     MDLNQFISIR RELHQIPETG YKEWKTQAYL LDYINKLPSR YLEVKKWRTG LLVRVSGTSP
     TKTIGYRTDI DALPITEETG LAFESKHAGN MHACGHDLHM SIALGVLTHF ASKPAKDNLL
     FVFQPAEEGP GGAKPIMESA EFAEWRPDSI YGLHIAPEYK VGQIAIKPGL LFANTSELFI
     SFKGKGGHAA YPHLANDMVV AASAFVGQMQ TIISRNIDPM DSAVITIGRI HGGEIQNVIA
     ETAFLDGTIR TLSPETMEIV WTRLKQLAKG WEEAYQCEVT FHAGSDYYQV DNDPAETAAF
     IDFLKESYPK SYVPAKSAMT GEDFGYFLSG IKGFMFWLGV DSEYSLHHAK LNPKEEAIPF
     AIEVLIHFLE SK