ID G9ZNT1_9LACO Unreviewed; 386 AA.
AC G9ZNT1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=N-acetyldiaminopimelate deacetylase {ECO:0000256|HAMAP-Rule:MF_01692};
DE EC=3.5.1.47 {ECO:0000256|HAMAP-Rule:MF_01692};
GN ORFNames=HMPREF9103_01385 {ECO:0000313|EMBL:EHL98695.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL98695.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHL98695.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHL98695.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC diaminopimelate and acetate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01692}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC acetyldiaminopimelate deacetylase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01692}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHL98695.1}.
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DR EMBL; AGEY01000064; EHL98695.1; -; Genomic_DNA.
DR RefSeq; WP_008212468.1; NZ_JH414960.1.
DR AlphaFoldDB; G9ZNT1; -.
DR STRING; 797515.HMPREF9103_01385; -.
DR PATRIC; fig|797515.3.peg.1283; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR UniPathway; UPA00034; UER00024.
DR Proteomes; UP000004625; Unassembled WGS sequence.
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 CDD; cd05670; M20_Acy1_YkuR-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF98; N-ACETYLDIAMINOPIMELATE DEACETYLASE; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692};
KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01692, ECO:0000313|EMBL:EHL98695.1};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01692}.
FT DOMAIN 182..278
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01692"
SQ SEQUENCE 386 AA; 42622 MW; 65E51F018644E07E CRC64;
MAQLTTDDLI EIRRHLHEHP ELAMHEVTTH QYLLTIIQKF KQDYLEIREL PDLPTALMVS
VRGSQPKRTI GYRTDIDALP VTEETGLPFA SQNPGVMHAC GHDIHMTVAL GVLNWFSEHQ
PEDNLVFFFQ PAEESENGGK VAYEQGVFEG KWRPDEFYGL HDNPNLPAGA IGCRMGTLFA
GTTEVNVDLI GKSGHAAYPQ DANDMVVAAA EFIGQVQTIV SRSVNPIEGG VITFGKLDAG
TIRNVIAGKA RIEGTIRGLT QKMIEHIVDR LKQVANGVAT SYDAKVDIEF NQGGYLPVEN
NDELTKRFID FAKQDPQTQF VETQPAMTGE DFGYLLSKIP GTMFWLGVDS SSPLHSATLN
PKESAIGKGV NSIVRFLRFR QGESIS
//
