ID F6IWE0_LACPE Unreviewed; 384 AA.
AC F6IWE0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=N-acetyldiaminopimelate deacetylase {ECO:0000256|HAMAP-Rule:MF_01692};
DE EC=3.5.1.47 {ECO:0000256|HAMAP-Rule:MF_01692};
GN ORFNames=LPE_01980 {ECO:0000313|EMBL:CCB82953.1};
OS Lactiplantibacillus pentosus MP-10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1028490 {ECO:0000313|EMBL:CCB82953.1};
RN [1] {ECO:0000313|EMBL:CCB82953.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP-10 {ECO:0000313|EMBL:CCB82953.1};
RX PubMed=21705590; DOI=10.1128/JB.05171-11;
RA Abriouel H., Benomar N., Perez Pulido R., Canamero M.M., Galvez A.;
RT "Annotated genome sequence of Lactobacillus pentosus MP-10, which has
RT probiotic potential, from naturally fermented Alorena green table olives.";
RL J. Bacteriol. 193:4559-4560(2011).
CC -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC diaminopimelate and acetate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01692}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC acetyldiaminopimelate deacetylase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01692}.
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DR EMBL; FR871814; CCB82953.1; -; Genomic_DNA.
DR RefSeq; WP_050339330.1; NZ_FLYG01000003.1.
DR AlphaFoldDB; F6IWE0; -.
DR GeneID; 49394445; -.
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 CDD; cd05670; M20_Acy1_YkuR-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF98; N-ACETYLDIAMINOPIMELATE DEACETYLASE; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692};
KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01692, ECO:0000313|EMBL:CCB82953.1};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692}.
FT DOMAIN 180..279
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 74
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
SQ SEQUENCE 384 AA; 42045 MW; 9C678994E367AE3F CRC64;
MVLRETDLIP IYQHLHQIPE IGLQEHETQA YLLSIIAKMP QDWLTVKTIS TLDTAILVKV
SGQRHDYRIG YRTDIDALPV TENTGLPFAS THPGVMHACG HDIHMSVALG ILSYFAENRP
ETDMIFMFQP AEENASGGQR LYESGALDGD WMPDEIFAFH DNPNLPTGAI GCRMGTLFAG
TCEIHAHLSG KSGHAAYPHQ ANDMVVAGAA LVSQLQTIVA RNVDPIQSGV VTLGHFSAGT
IGNVIAGEAQ IDGTIRALTQ EMNLHIQRRV RTIAEGVALA YDCNIDLKLN QGGYYPVENN
DAITSDFIQY MQDDADVNFI ETAPAMTGED FGYLIHQIPG TMFWLGVDSP YSLHSENMVP
HTAAIMSGVN AMTGYLTHRN ALRK
//
