DAPEL_GEOKA
ID DAPEL_GEOKA Reviewed; 377 AA.
AC Q5L145;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=GK1050;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000043; BAD75335.1; -; Genomic_DNA.
DR RefSeq; WP_011230550.1; NC_006510.1.
DR AlphaFoldDB; Q5L145; -.
DR SMR; Q5L145; -.
DR STRING; 235909.GK1050; -.
DR MEROPS; M20.A27; -.
DR EnsemblBacteria; BAD75335; BAD75335; GK1050.
DR KEGG; gka:GK1050; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000001172; 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..377
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_0000376755"
FT ACT_SITE 70
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ SEQUENCE 377 AA; 41763 MW; A9353545DC146B18 CRC64;
MSAISPFVAI RRDLHQIPEL GFQEFKTQQY LLRYIQSLPQ ERLQVRTWKT GIFVKVNGTS
PRKTIGYRAD MDGLPIREET GLPYRSKHEG RMHACGHDVH MSIALGVLTH FAHHPLKDDL
LFVFQPAEEG PGGAKPMLES DIMREWKPDI IVALHIAPEY PVGTIATKEG LLFANTSELF
IDLKGKGGHA AFPHLANDMV VAACALVTQL QSIVARNVDP LDSAVITIGK IAGGTVQNVI
AEHARLEGTI RTLSTAAMQK VKRRIEAIVH GIEVAYECEA SIDYGAMYHE VYNDPDLTAE
FMKFAKAHGG VNVIRCKEAM TGEDFGYMLA DIPGFMFWLG VASPYGLHHA KLAPNEEAID
RAIAFLIDYF SWKGNAE