DAPEL_LACLM
ID DAPEL_LACLM Reviewed; 376 AA.
AC A2RI06;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=llmg_0292;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL96899.1; -; Genomic_DNA.
DR RefSeq; WP_011834362.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI06; -.
DR SMR; A2RI06; -.
DR STRING; 416870.llmg_0292; -.
DR EnsemblBacteria; CAL96899; CAL96899; llmg_0292.
DR KEGG; llm:llmg_0292; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR PhylomeDB; A2RI06; -.
DR BioCyc; LLAC416870:LLMG_RS01525-MON; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000000364; 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..376
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376766"
FT ACT_SITE 69
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 376 AA; 41751 MW; 649BC3375263F129 CRC64;
MINLIEIRRQ LHQIPEIGLE EHKTQKYLLT IIHQIIQNKS FIQVETWQTG LLVYLKGSQG
QKTIGWRTDI DGLPVEELTN LPFASKNGRM HACGHDIHMT VALGLLEKLS ESQPKNNLLF
LFQPAEENEA GGKLMYDGGA FKNWLPDEFY GLHVRPDLKV GDIATNEQTL FAGTCEVELT
FVGTGGHAAF PHTANDALVA AAYFVTQVQT IVSRNVDPLD SAVVTFGKME AGTTNNIIAE
RAFLHGTIRS LTQEVNELTQ KRLTELAKGV AQSFDMTIDL KLKQGGYLPV ENNPKLAKEL
MDFFRNETKA NLIDIAPAMT GEDFGYLLSK IPGVMFWLGI NSEAPLHSQK MQADEGVLDF
AVEAIGQFLD IKANRN