(data stored in ACNUC9435 zone)

SWISSPROT: DAPEL_LISIN

ID   DAPEL_LISIN             Reviewed;         371 AA.
AC   Q92D10;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 98.
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=lin1011;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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-LL-2,6-diaminoheptanedioate = acetate + LL-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:20405, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57609, ChEBI:CHEBI:58767; EC=3.5.1.47;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; AL596167; CAC96242.1; -; Genomic_DNA.
DR   PIR; AB1559; AB1559.
DR   RefSeq; WP_003761548.1; NC_003212.1.
DR   STRING; 272626.lin1011; -.
DR   MEROPS; M20.A27; -.
DR   EnsemblBacteria; CAC96242; CAC96242; CAC96242.
DR   KEGG; lin:lin1011; -.
DR   eggNOG; ENOG4105CH2; Bacteria.
DR   eggNOG; COG1473; LUCA.
DR   HOGENOM; HOG000241404; -.
DR   KO; K05823; -.
DR   OMA; RAHACGH; -.
DR   OrthoDB; 796259at2; -.
DR   BioCyc; GCF_000195795:LIN_RS05165-MONOMER; -.
DR   UniPathway; UPA00034; UER00024.
DR   Proteomes; UP000002513; 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: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;
DR   PRODOM; Q92D10.
DR   SWISS-2DPAGE; Q92D10.
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis.
FT   CHAIN           1..371
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000376771"
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   371 AA;  41546 MW;  7694A5905A5B070B CRC64;
     MLNEFIAIRR DLHQIPETGY KELKTQAYLL DYISKLPNEF LEIKKWRTGI LVLVKGTNPG
     KTIGYRTDID ALPITEETGL PFESKHAGNM HACGHDLHMS IALGVLTHFA SKPAKDNLLF
     VFQPAEEGPG GAKPIMESAE FSEWRPDTIY GLHIAPEYKV GQIAIKPGLL FANTSELFIS
     FKGKGGHAAY PHLANDMVVA ASAFVGQMQT IISRNIDPMD SAVITIGRIH GGEIQNVIAE
     TAFLDGTIRT LSPETMEIVW TRLKQLAKGW EEAYQCEVEF HPGSDYYQVD NDPVETEEFI
     HFLEEQYPES YVPARSAMTG EDFGYFLSEI KGFMFWLGVD SEYSLHHAKL SPKEEAIPFA
     IDVLVNFLES K
//

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