ID   DAPEL_STRTD             Reviewed;         377 AA.
AC   Q03IN1;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=N-acetyldiaminopimelate deacetylase {ECO:0000255|HAMAP-Rule:MF_01692};
DE            EC=3.5.1.47 {ECO:0000255|HAMAP-Rule:MF_01692};
GN   OrderedLocusNames=STER_1813;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR   EMBL; CP000419; ABJ66941.1; -; Genomic_DNA.
DR   RefSeq; WP_011681671.1; NC_008532.1.
DR   AlphaFoldDB; Q03IN1; -.
DR   SMR; Q03IN1; -.
DR   KEGG; ste:STER_1813; -.
DR   HOGENOM; CLU_023257_0_1_9; -.
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..377
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000376793"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ   SEQUENCE   377 AA;  41765 MW;  BE1E04F073D50B4C CRC64;
     MTLDLIKIRR DLHQIPEIGL EEFKTQAYLL ERIAEMTEGK DFVEQRTWRT GILVFLHGSA
     PEKTIGWRTD IDGLPIVEET GLDFKSIHEG RMHACGHDIH MTTALGLLDQ MLQVQPKNNM
     LFLFQPAEEN EAGGMLMYED GAFGDWLPDE FYGLHVRPDF KVGDIATNTN TLFAGTCEVL
     VTFKGKGGHA AFPHEANDAL VAASYFITQV QTIVSRNVDP IQGGVVTFGS FHAGTTNNVI
     AETAEVYGTI RTLTQEMSLL IQKRVRQIAE GVAASFGMEV DIMLKQGGYL PVENNPALAK
     ELMAFFDASP MVNLIDCLPA MTGEDFGYLL SKVPGVMFWL GIDTPYALHH PKMSPNEEAL
     AFAVSEIGKF LKYKAED