ID   DAPEL_PRIM1             Reviewed;         375 AA.
AC   D5E0A1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=N-acetyldiaminopimelate deacetylase;
DE            EC=3.5.1.47 {ECO:0000305|PubMed:4962540};
GN   OrderedLocusNames=BMQ_1331;
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=545693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
RN   [2]
RP   FUNCTION AS A N-ACETYLDIAMINOPIMELATE DEACETYLASE AND IN LYSINE
RP   BIOSYNTHESIS, AND CATALYTIC ACTIVITY.
RX   PubMed=4962540; DOI=10.1016/s0021-9258(18)95843-6;
RA   Sundharadas G., Gilvarg C.;
RT   "Biosynthesis of alpha,epsilon-diaminopimelic acid in Bacillus
RT   megaterium.";
RL   J. Biol. Chem. 242:3983-3984(1967).
CC   -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC       diaminopimelate and acetate. {ECO:0000269|PubMed:4962540}.
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;
CC         Evidence={ECO:0000305|PubMed:4962540};
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.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC       acetyldiaminopimelate deacetylase subfamily. {ECO:0000305}.
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DR   EMBL; CP001983; ADE68364.1; -; Genomic_DNA.
DR   RefSeq; WP_013056039.1; NC_014019.1.
DR   AlphaFoldDB; D5E0A1; -.
DR   SMR; D5E0A1; -.
DR   STRING; 545693.BMQ_1331; -.
DR   MEROPS; M20.A27; -.
DR   EnsemblBacteria; ADE68364; ADE68364; BMQ_1331.
DR   GeneID; 64144700; -.
DR   KEGG; bmq:BMQ_1331; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   OMA; RAHACGH; -.
DR   OrthoDB; 796259at2; -.
DR   UniPathway; UPA00034; UER00024.
DR   Proteomes; UP000000935; Chromosome.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN           1..375
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000408258"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  42228 MW;  A6E93DCB4D6EEC32 CRC64;
     MAENEFVKIR RELHKIPELG FQEVKTQRFL LDYINTLPQE RLEVKTWKTG LFVKVHGTNP
     TKTIGYRADI DGLPITEETN YSFQSQHEGL MHACGHDMHM AIGLGVLTYF AQHEIKDNVL
     FIFQPAEEGP GGAQPMLQSD IMKEWLPDFI FALHVAPEYP VGSIALKEGL LFANTSELFI
     DLKGKGGHAA YPHTTNDMVV AACQLVSQLQ TIVARNVDPL DSAVITVGKI QGGTVQNIIA
     ERARIEGTIR TLSPESMTRV KERIEAIVKG VEVGYQCETA IDYGCMYHQV YNHHEVTREF
     MEFAKEQTDV DVIECKEAMT GEDFGYMLKD IPGFMFWLGV QSEYGLHHAK LQPHEGAIDI
     AISLITKYFE HKGNQ