ID A0A0R2JMI5_9LACO Unreviewed; 387 AA.
AC A0A0R2JMI5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=IV52_GL001173 {ECO:0000313|EMBL:KRN78403.1};
OS Fructilactobacillus lindneri DSM 20690 = JCM 11027.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN78403.1, ECO:0000313|Proteomes:UP000051565};
RN [1] {ECO:0000313|EMBL:KRN78403.1, ECO:0000313|Proteomes:UP000051565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN78403.1,
RC ECO:0000313|Proteomes:UP000051565};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(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}.
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:KRN78403.1}.
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DR EMBL; JQBT01000034; KRN78403.1; -; Genomic_DNA.
DR RefSeq; WP_054646770.1; NZ_MIYK01000010.1.
DR AlphaFoldDB; A0A0R2JMI5; -.
DR STRING; 53444.AYR59_02265; -.
DR GeneID; 61249700; -.
DR PATRIC; fig|1122148.6.peg.1200; -.
DR OrthoDB; 9776731at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000051565; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051565}.
FT DOMAIN 183..277
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 76
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
SQ SEQUENCE 387 AA; 42835 MW; 2534217CFEAFE042 CRC64;
MGEAKTDLLK IYRNLHQIPE LALHEFQTHD YLMKQIKQDT AAIDYAEIQV PNELPTAILV
LLHGTQPKRT IGYRTDIDAL PVAEDTGLDF SSKHDGVMHA CGHDIHMTVA LGVLQYFTQH
QPTDNLLFFF QPAEESENGG KLAYEDGIFT GKWKPDEFYG LHDNPQLSAG AIGCRMGTLF
AGTTEVDVDF TGTQGHAAYP QFANDMIVAA SQFINQVQTI VSRSVDPIEG GVITFGQFNA
GTIRNVISGS AHLKGTIRGL TQKMIEHIDE RLQAVAKGIE TSYDCQVDLK LNQGGYLPVE
NNDKLTADFI NYMEENPKVD YVETEPAMTG EDFGYLLAKF PGTMFWLGIG DPKNQLHSSK
LVPDTNAIQP GIDAITGFLQ HRMLEKD
//
