DAPEL_LIMF3
ID DAPEL_LIMF3 Reviewed; 384 AA.
AC B2GC10;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=LAF_0856;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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; AP008937; BAG27192.1; -; Genomic_DNA.
DR RefSeq; WP_012391181.1; NC_010610.1.
DR AlphaFoldDB; B2GC10; -.
DR SMR; B2GC10; -.
DR EnsemblBacteria; BAG27192; BAG27192; LAF_0856.
DR GeneID; 61200229; -.
DR KEGG; lfe:LAF_0856; -.
DR PATRIC; fig|334390.5.peg.942; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR OrthoDB; 796259at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000001697; Chromosome.
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..384
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376760"
FT ACT_SITE 73
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 384 AA; 42004 MW; F90F8280CFADED80 CRC64;
MLGTEELIQI RHHLHQIPEL ALQETETHAY LMEVIGKMEQ DHLEILEPED LPTAILVRVN
GTAPVRTIGY RTDIDALPVQ EETGLPYAST HSGVMHACGH DVHMTVALGV LDYFASHQPK
DNLLFFFQPA EESEAGGQRA YELGLFEGKW RPDEFYGLHD NPALKTGVIG CRLGTLFAGT
TEVDIDVLGK DGHAAFPQEA NDAVVAAAAL IMQVQTIISR SINPVEAGVI TLGKLEAGTI
RNVIAGHARI EGTIRGLTQE MIETIDRRLQ DVCEGIAKSF GVTVNLALNQ GGYLPVENDP
ALTKRFINFM QNNPAVDYVE TAPAMTGEDF GYLLSKFPGT MFWLGVEDDA QLHQATLTPN
EGAIQKGIDA LTSFITYRSQ AEED