(data stored in ACNUC7421 zone)

HOGENOM: LIMON1_1_PE1004

ID   LIMON1_1_PE1004                      STANDARD;      PRT;   371 AA.
AC   LIMON1_1_PE1004; Q8Y8A0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=N-acetyldiaminopimelate deacetylase; EC=3.5.1 47;
DE   (LIMON1_1.PE1004).
GN   OrderedLocusNames=lmo1012;
OS   LISTERIA MONOCYTOGENES EGD-E.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LIMON1_1.PE1004.
CC       Listeria monocytogenes EGD-e, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:DAPEL_LISMO
CC   -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC       diaminopimelate and acetate (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-acetyl-LL-2,6-diaminoheptanedioate + H(2)O =
CC       acetate + LL-2,6-diaminoheptanedioate.
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.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC       acetyldiaminopimelate deacetylase subfamily.
CC   -!- GENE_FAMILY: HOG000241404 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8Y8A0; -.
DR   EMBL; AL591977; CAC99090.1; -; Genomic_DNA.
DR   PIR; AD1201; AD1201.
DR   RefSeq; NP_464537.1; NC_003210.1.
DR   HSSP; P54970; 1XMB.
DR   ProteinModelPortal; Q8Y8A0; -.
DR   GeneID; 986510; -.
DR   GenomeReviews; AL591824_GR; lmo1012.
DR   KEGG; lmo:lmo1012; -.
DR   GenoList; LMO1012; -.
DR   OMA; ARELHIT; -.
DR   ProtClustDB; CLSK2753188; -.
DR   BioCyc; LMON169963:LMO1012-MON; -.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:EC.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01692; DapEL; 1; -.
DR   InterPro; IPR023905; AcetylDAP_deacetylase.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Peptidase_M20_dimer; 1.
DR   TIGRFAMs; TIGR01891; Amidohydrolases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; FALSE_NEG.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; FALSE_NEG.
DR   HOGENOMDNA; LIMON1_1.PE1004; -.
KW   hypothetical protein;
KW   Amino-acid biosynthesis; Complete proteome;
KW   Diaminopimelate biosynthesis; Hydrolase; Lysine biosynthesis;
KW   Reference proteome.
SQ   SEQUENCE   371 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLNEFIAIRR ELHQIPETGY KELKTQAYLL DYISKLPSGH LEVKKWRTGI LVLVKGTNPE
     KTIGYRTDID ALPITEETEL PFASKHPGNM HACGHDLHMS IALGVLTHFA SKPAKDNLLF
     VFQPAEEGPG GAKPIMESTE FAEWRPDSIY GLHIAPEYKV GEIAIKPGLL FANTSELFIS
     FKGKGGHAAY PHLANDMVVA ASAFVGQMQT IISRNIDPMD SAVITIGRIH GGEIQNVIAE
     TAYLDGTIRT LSPETMEIVW TRLKQLAKGW EEAYQCEVEF HPGSDYYQVD NDPVETEEFI
     HFLEEQYPES YVPARSAMTG EDFGYFLSEI KGFMFWLGVD SEYSLHHAKL NPKEEAIPFA
     IDVLIHFLES K
//

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