ID A0A075JPT8_9BACI Unreviewed; 373 AA.
AC A0A075JPT8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=X953_12735 {ECO:0000313|EMBL:AIF43909.1};
OS Virgibacillus sp. SK37.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF43909.1, ECO:0000313|Proteomes:UP000027985};
RN [1] {ECO:0000313|EMBL:AIF43909.1, ECO:0000313|Proteomes:UP000027985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK37 {ECO:0000313|EMBL:AIF43909.1,
RC ECO:0000313|Proteomes:UP000027985};
RA Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT halophilic bacterium isolated from Thai fish sauce fermentation.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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; CP007161; AIF43909.1; -; Genomic_DNA.
DR RefSeq; WP_040955807.1; NZ_CP007161.1.
DR AlphaFoldDB; A0A075JPT8; -.
DR STRING; 403957.X953_12735; -.
DR MEROPS; M20.A27; -.
DR KEGG; vir:X953_12735; -.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OrthoDB; 9776731at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000027985; 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};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692};
KW Reference proteome {ECO:0000313|Proteomes:UP000027985}.
FT DOMAIN 180..269
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 69
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
SQ SEQUENCE 373 AA; 41539 MW; D117FDB6F1FB69B6 CRC64;
MKLSELQKIR RDLHQIPELG FQENKTQRYL LDKIDAMATE NVTVKRWKTG ILVKVNGFSP
DKMIGFRCDI DGLPITEKTD FTFSSTHDGK MHACGHDFHM TIALGALQTI IDQPIKDDML
FIFQPAEEGP GGALPMMNSN EFLKWKPDVI FALHIAPELP VGTVSSKQGL LFANTSELFI
DFKGKGGHAA YPHLTNDMTV AASNFVVQLQ QIVSRAINPL ESAVVTIGKM ESGFVQNAIA
ETARLEGTIR TLNPETIQIV KDRIENMAKG FEVSSDCTIE IDYGSNYYQV FNQKKYVDIF
NKTMEASGIH YKEANAAMTG EDFGYMLKEI PGFMFWLGVD SSYGLHHAKL NPDERAIEVG
VKSVSAMIQS LSL
//
