ID   DAPEL_BACCR             Reviewed;         376 AA.
AC   Q819J6;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=BC_3980;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP10900.1; -; Genomic_DNA.
DR   RefSeq; NP_833699.1; NC_004722.1.
DR   RefSeq; WP_000218674.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q819J6; -.
DR   SMR; Q819J6; -.
DR   STRING; 226900.BC_3980; -.
DR   MEROPS; M20.A27; -.
DR   EnsemblBacteria; AAP10900; AAP10900; BC_3980.
DR   KEGG; bce:BC3980; -.
DR   PATRIC; fig|226900.8.peg.4106; -.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   OMA; RAHACGH; -.
DR   UniPathway; UPA00034; UER00024.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IBA:GO_Central.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..376
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000376740"
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   376 AA;  42200 MW;  B7D6116B91E8BA5E CRC64;
     MTVSKFVQIR RDLHRIPEIG FKEWKTQQYI LDYIGTLSHE FVEVKTWKTG VIVKVNGKNP
     EKIIGYRADI DGLPITEETG YEFASIHEGM MHACGHDVHT TIGLGLLTKA VSERIDDDLV
     FLFQPAEEGP GGALPMLESE ELKEWKPNII LGLHIAPEYA VGTIATKEGL LFANTSELYI
     DLKGKGGHAA YPHTANDMIV AASHLVTQLQ SVISRNVNPL DSAVITIGKI TGGTVQNIIA
     EKSRLEGTIR TLSVESMKRV KSRIESIVAG IEASFQCEVI IDYGAMYHQV YNHEELTREF
     MEFVHKQTDM NVITCTEAMT GEDFGYMLRE IPGFMFWLGV NSEYGLHHAK LKPDEEVIEK
     AITFLSQYVK WKGNRK