ID F9P1U0_STRMT Unreviewed; 376 AA.
AC F9P1U0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=HMPREF9178_1129 {ECO:0000313|EMBL:EGR93778.1};
OS Streptococcus mitis bv. 2 str. F0392.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=768726 {ECO:0000313|EMBL:EGR93778.1, ECO:0000313|Proteomes:UP000003771};
RN [1] {ECO:0000313|EMBL:EGR93778.1, ECO:0000313|Proteomes:UP000003771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0392 {ECO:0000313|EMBL:EGR93778.1,
RC ECO:0000313|Proteomes:UP000003771};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (JUL-2011) 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}.
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:EGR93778.1}.
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DR EMBL; AFUO01000001; EGR93778.1; -; Genomic_DNA.
DR RefSeq; WP_000885090.1; NZ_AFUO01000001.1.
DR AlphaFoldDB; F9P1U0; -.
DR PATRIC; fig|768726.4.peg.1063; -.
DR eggNOG; COG1473; Bacteria.
DR OrthoDB; 9776731at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000003771; 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, ECO:0000313|EMBL:EGR93778.1};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692}.
FT DOMAIN 174..267
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 376 AA; 41667 MW; FEEC8DEFEBD527F1 CRC64;
MLDLIQTRRD LHQIPEIGLE EFKTQAYLLA VIEKLTADKN FVQVRTWRTG ILVYLQGSQP
ERTIGWRTDI DGLPIVEQTD LPFSSQHQGR MHACGHDFHM TIALGCLERA LEEQPKNNLL
FLFQPAEENE AGGMLMYEDG AFGDWLPDKF YGLHVRPDLK VGQIATNTHT LFAGTCEVKI
RFKGKGGHAA FPHEANDALV AASYFVTQVQ SVVSRNVNPI EGAVVTFGVF QAGTTNNVIT
DTAFLHGTIR ALTQDMSLLV QKRVKTVAEG VATAFGMEVE VELKQGGYLP VENNPALARE
LMDFFEEKDG IELIDIEPAM TGEDFGYLLS KVDGVMFWLG IDSPYALHHP QMSPKEEALA
IGVDAVSSFL KKKAAE
//
