DAPEL_EXIS2
ID DAPEL_EXIS2 Reviewed; 370 AA.
AC B1YJ90;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Exig_2019;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) 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; CP001022; ACB61471.1; -; Genomic_DNA.
DR RefSeq; WP_012370889.1; NC_010556.1.
DR AlphaFoldDB; B1YJ90; -.
DR SMR; B1YJ90; -.
DR STRING; 262543.Exig_2019; -.
DR MEROPS; M20.A27; -.
DR EnsemblBacteria; ACB61471; ACB61471; Exig_2019.
DR KEGG; esi:Exig_2019; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR OrthoDB; 796259at2; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000001681; 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..370
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376754"
FT ACT_SITE 67
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 370 AA; 41340 MW; B0D34BB64655EA85 CRC64;
MEYAIEMRRE LHKIPEPGFK EFKTQAFILD QIRSYPEDRV SYDTFETGVF VRVKGLTGNR
TIGYRADIDG LPIEEATGLP FCSEHPGFMH ACGHDVHASI ALGLLRRIVE LPVMDDVVFL
FQPAEEGPGG AEPMIKSPLF EKYRPSEMYG LHVAPEYPVG TIASRPGVLF ASAREVHITI
YGQSGHAAFP HLTIDTVVAQ AALIMQLQTI VSRSINPMNC SVITIGKVDA GIRENVIAGR
ALLDGTMRAL NGTDMEKLEQ RVRDIIRGIE ASFGVKIDLQ FGNRYYEVVN DQRVVDKFSS
FVKMNANYIE CDAAMTGEDF GFMLKEIPGM MFWLGVNNAT SGLHQPTLNP DEEAIPFVIN
LLDHYFREYV