DAPEL_LACCB
ID DAPEL_LACCB Reviewed; 383 AA.
AC B3W7E6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=LCABL_00980;
OS Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=543734;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL23;
RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA Deutscher J.;
RT "Lactobacillus casei BL23 complete genome sequence.";
RL Submitted (JUN-2008) 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}.
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DR EMBL; FM177140; CAQ65230.1; -; Genomic_DNA.
DR RefSeq; WP_003604079.1; NC_010999.1.
DR AlphaFoldDB; B3W7E6; -.
DR SMR; B3W7E6; -.
DR KEGG; lcb:LCABL_00980; -.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR OrthoDB; 796259at2; -.
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 PANTHER; PTHR11014; PTHR11014; 1.
DR PANTHER; PTHR11014:SF98; PTHR11014:SF98; 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..383
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376759"
FT ACT_SITE 72
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 383 AA; 42065 MW; 387FEEF6B7469A58 CRC64;
MKEADLITLR RQLHQIPELA LQEKETHALL LKTIQGLPQT YLTIRTLPDL PTALLVKVQG
RDPQRTIGYR TDIDALPVTE KTGLPFASKH SGIAHACGHD IHMTVALGIL SYFAEHQPKD
NLIFFFQPAE ESKNGGKLAY DMGAFTGDWH IDEFYGLHDR PDLPAGTIST RLGTLFAGTT
EINVDLIGKS GHAALPQNAN DMIVAAASFI SQIQTVVARN VGPTDSAVIT FGLMRAGTIR
NVIAGRAHLE GTLRGFTQQQ IDFLQQRIRD IGQGIAASFN CQVKVALNQG GYYPVENNDK
LTKDFIQVMK DDPDVTFVDT KPVMTGEDFG YLLNKIPGTM FWLGVNDPDS QLHAADFSPD
EAALVPGVTA VVHFLEHRML EKV