DAPEL_LACAC
ID DAPEL_LACAC Reviewed; 383 AA.
AC Q5FKR0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=LBA0853;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42714.1; -; Genomic_DNA.
DR RefSeq; WP_003546881.1; NC_006814.3.
DR RefSeq; YP_193745.1; NC_006814.3.
DR AlphaFoldDB; Q5FKR0; -.
DR SMR; Q5FKR0; -.
DR STRING; 272621.LBA0853; -.
DR EnsemblBacteria; AAV42714; AAV42714; LBA0853.
DR GeneID; 56942481; -.
DR KEGG; lac:LBA0853; -.
DR PATRIC; fig|272621.13.peg.815; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR BioCyc; LACI272621:G1G49-864-MON; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000006381; 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; Reference proteome.
FT CHAIN 1..383
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376757"
FT ACT_SITE 75
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 383 AA; 42314 MW; 91D7ED97AB3789F1 CRC64;
MTVLSEKELI QIRRHLHEIP ELALQEKETH DYLLKVIKNL KQDHLTIVVP KTLPTAILGL
VKGINPKKTI GYRTDIDALP VQEKTGLPFT SKHSGIMHAC GHDIHMTVAL GLLSYFSENQ
PKDNLLFFFQ PAEESESGGK QAYEKGLFQG KFKPDEFYGL HDNPELPAGS IGCRMGTLFA
GTTEINIDVI GKSGHAAFPQ NANDTVVAAA NLIMQIQTII SRSIDPIQSG VITLGKVNAG
VIRNVIAGHT RIEGTIRGLT QKMILQIDRR LQDVCDGIAH SYNVEVNLEL NQGGYWPVEN
DPKITKNFIS YMKKNPKVNF IETEPKMTGE DFGFLLAKFP GTMFWLGVGD PSSQLHSSTL
NPDEKSIQSG IDAIKGFLID RMG