DAPEL_ALKCK
ID DAPEL_ALKCK Reviewed; 374 AA.
AC Q5WF94;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=ABC2431;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD64966.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5WF94; -.
DR SMR; Q5WF94; -.
DR STRING; 66692.ABC2431; -.
DR MEROPS; M20.A27; -.
DR EnsemblBacteria; BAD64966; BAD64966; ABC2431.
DR KEGG; bcl:ABC2431; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000001168; 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..374
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376746"
FT ACT_SITE 68
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 374 AA; 41083 MW; 921C2C44C0479216 CRC64;
MKMNDLIHIR RAFHQIPELG FNEFKTQKLL LDTISNMEQT RLQIKTWKTA VFVRVEGRQD
YTIAYRADMD GLPITEETGY SFASKHEGAM HACGHDFHMT IALGLLDHFA SHEPECHLLF
IFQPAEEGPG GAKPIIEADV LGAWQPDEIY ALHIDPNLPV GSIATKPGLL FANTSELFID
FQGKGGHAAY PHTANDMVVA CAHFVTQVQT VVARNIDPLD SAVVTLGVIA GGTKQNVIAA
TARLEGTIRT LSMASMEVVK SRLEAIAAGI EASFACKIAI DYGSNYCEVY NDPELAEAFA
AFSKTRKGIT FVEAEEAMTG EDFGYFLKQY PGVMFWLGVD SPYGLHDSRL QPSEEAIGIA
IEHMVAFLSA KKPR