ID W6T7I0_9LACO Unreviewed; 384 AA.
AC W6T7I0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=LFAB_10220 {ECO:0000313|EMBL:ETY73823.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY73823.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY73823.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY73823.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETY73823.1}.
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DR EMBL; AWWK01000048; ETY73823.1; -; Genomic_DNA.
DR RefSeq; WP_024625129.1; NZ_KK036500.1.
DR AlphaFoldDB; W6T7I0; -.
DR STRING; 1400520.LFAB_10220; -.
DR PATRIC; fig|1400520.3.peg.1994; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OrthoDB; 9776731at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000019247; Unassembled WGS sequence.
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};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692}.
FT DOMAIN 180..280
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; 41968 MW; 6D5ED6C81CA67753 CRC64;
MALRETDLIP IYQHLHQIPE LGLEEHETQA YLLSLIAKMP QDLLTIKKVP AVDTAILVKV
SGRKHDYRIG YRTDIDGLPV TEATGLPFAS THPGKMHACG HDIHMSVALG ILSYFAENQP
ATDMIFIFQP AEENASGGMR LYQSGALSGD WLPDEIFAFH DNPDLPAGAI GCRMGTLFAG
TCEIHAHLTG KSGHAAFPHN ANDMVVAGSA LVQQLQTIVS RNVDPIQSGV VTLGHFTAGT
IGNVIAGEAQ IDGTIRALTQ DMNEHIQRRV RTIVEGIALA YDCNIDLDLH QGGYYPVENN
DQITADFIDY MQTDDDVNFI ETRPAMTGED FGYLIHQIPG TMFWLGVDSP YSLHSEHMVP
HTSAIMAGVD AMTGYLTHRN ALVK
//