ID A0A068LNY3_BACMM Unreviewed; 377 AA.
AC A0A068LNY3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-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 Name=dapL {ECO:0000313|EMBL:AIE59481.1};
GN ORFNames=BMMGA3_05255 {ECO:0000313|EMBL:AIE59481.1};
OS Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE59481.1, ECO:0000313|Proteomes:UP000027602};
RN [1] {ECO:0000313|EMBL:AIE59481.1, ECO:0000313|Proteomes:UP000027602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX PubMed=25758049;
RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT previously uncharted transcriptional landscape.";
RL BMC Genomics 16:73-73(2015).
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; CP007739; AIE59481.1; -; Genomic_DNA.
DR RefSeq; WP_034669538.1; NZ_CP007739.1.
DR AlphaFoldDB; A0A068LNY3; -.
DR STRING; 796606.BMMGA3_05255; -.
DR MEROPS; M20.A27; -.
DR KEGG; bmet:BMMGA3_05255; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OrthoDB; 9776731at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000027602; 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 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:AIE59481.1};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692};
KW Reference proteome {ECO:0000313|Proteomes:UP000027602}.
FT DOMAIN 182..271
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
SQ SEQUENCE 377 AA; 42785 MW; 529CB8A5FEE1DE56 CRC64;
METMTSPFVK IRRDLHQIPE LGFQEFKTQR YLLNYLQSLP QEAIEIKKWK TGLFVKVNGK
NPRKTIGYRT DIDGLPITEE TELPYRSLHE GNMHACGHDF HMSIALGLVT YFAKNPIDDH
LLFIFQPAEE GPGGAEPMLK SEIMQEWKPD LIFALHIAPE YPVGAIALKK GLLFANTSEL
FIDLKGKGGH AAYPHQTKDM IVAACSLVTQ LQTVVARYVD PLDSAVITIG KITGGTVQNI
IAEKARLEGT IRTLSVDSMK RVKDRILSLI KGVEIGYECE VSVDFGSMYY QVYNEEKLTE
EFMDYMRNHT DIQVIECKEA MTGEDFGYML REIPGFMFWL GVESEYGLHH SKLNPNEAAI
EKAISFLTKY IEYKGNR
//
