DAPEL_GEOSW
ID DAPEL_GEOSW Reviewed; 376 AA.
AC C5D827;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=GWCH70_0945;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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; CP001638; ACS23808.1; -; Genomic_DNA.
DR RefSeq; WP_015863287.1; NC_012793.1.
DR AlphaFoldDB; C5D827; -.
DR SMR; C5D827; -.
DR STRING; 471223.GWCH70_0945; -.
DR MEROPS; M20.A27; -.
DR EnsemblBacteria; ACS23808; ACS23808; GWCH70_0945.
DR KEGG; gwc:GWCH70_0945; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OMA; RAHACGH; -.
DR OrthoDB; 796259at2; -.
DR UniPathway; UPA00034; UER00024.
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.
FT CHAIN 1..376
FT /note="N-acetyldiaminopimelate deacetylase"
FT /id="PRO_1000215932"
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 376 AA; 41928 MW; E403EAD6AC08B7C7 CRC64;
MSSISPFVAI RRDLHKIPEL GFQEFKTQQY LLRYIHALPQ ERLEIQTWKT GIFVKVKGTA
PRKMIGYRTD IDGLPIKEET GLPYSSEHEG NMHACGHDVH MSIALGLLTH FAEHPIQDDL
LFIFQPAEEG PGGAKPMLES EIMKVWKPDM ILALHIAPEY PVGTIATKEG LLFANTSELF
IDLKGKGGHA AFPHLANDMV VAACSLVTQL QSIVARNVDP LDSAVITIGK ISGGTVQNVI
AEHARLEGTI RTLSVDSMKK VKERIEAMVS GIKMAYQCEA EIDYGSMYHQ VYNDPELTTE
FIQFAENYQG IRFIRCKEAM TGEDFGYMLA EIPGFMFWLG VDSPYGLHHA KLTPNEAAID
QGISFLISYI TWKGNN