DAPEL_STRU0
ID DAPEL_STRU0 Reviewed; 376 AA.
AC B9DVY6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=N-acetyldiaminopimelate deacetylase {ECO:0000255|HAMAP-Rule:MF_01692};
DE EC=3.5.1.47 {ECO:0000255|HAMAP-Rule:MF_01692};
GN OrderedLocusNames=SUB1698;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
CC -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC diaminopimelate and acetate. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01692}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC acetyldiaminopimelate deacetylase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01692}.
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DR EMBL; AM946015; CAR43614.1; -; Genomic_DNA.
DR RefSeq; WP_015911991.1; NC_012004.1.
DR AlphaFoldDB; B9DVY6; -.
DR SMR; B9DVY6; -.
DR STRING; 218495.SUB1698; -.
DR EnsemblBacteria; CAR43614; CAR43614; SUB1698.
DR KEGG; sub:SUB1698; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR OrthoDB; 796259at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000000449; 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 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 PANTHER; PTHR11014; PTHR11014; 1.
DR PANTHER; PTHR11014:SF98; PTHR11014:SF98; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Hydrolase;
KW Lysine biosynthesis; Reference proteome.
FT CHAIN 1..376
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376795"
FT ACT_SITE 69
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 376 AA; 41600 MW; A23FB71C3153CCBE CRC64;
MLDLIAIRRQ LHQIPEIGLE EYQTQAFLLS VIEQLCQDKP FIQIKTWKTG ILVFLKGYAP
EKTVAWRSDM DGLPITEETG LAFASKHQGR MHACGHDIHM TMALGLLEAL VEKQSKHNML
FIFQPAEENE AGGMLMYQSG ALDEWMPDEV YALHVRPDLP VGTLASNRAT LFAGTCEVKV
SFKGKGGHAA FPHHANDALV AASYFVTQVQ TIVSRNVDPI EGAVVTFGSL HAGTTNNVIS
QEALLHGTIR TLTHDMSQLT QKRLTEMAEG IAKSFGLEVD VHLKQGGYLP VENNPELADE
LISFFKESDT INMIECLPAM TGEDFGFLLS KVKGVMFWLG VDTPYPLHHA KMSPDEGAIK
QALPEIKAFL EENIED