ID   E3G511_ENTCS            Unreviewed;       420 AA.
AC   E3G511;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   01-MAY-2013, entry version 17.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=Entcl_0888;
OS   Enterobacter cloacae (strain SCF1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=701347;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B.,
RA   Woo H., Hazen T.C., Woyke T.;
RT   "Complete sequence of Enterobacter cloacae SCF1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine +
CC       CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily.
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DR   EMBL; CP002272; ADO47160.1; -; Genomic_DNA.
DR   RefSeq; YP_003940444.1; NC_014618.1.
DR   EnsemblBacteria; ADO47160; ADO47160; Entcl_0888.
DR   GeneID; 9905908; -.
DR   KEGG; esc:Entcl_0888; -.
DR   PATRIC; 42595827; VBIEntClo171306_0909.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; AIDTEHY; -.
DR   BioCyc; ECLO701347:GH9V-903-MONOMER; -.
DR   UniPathway; UPA00034; UER00027.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP.
DR   Gene3D; 2.40.37.10; -; 1.
DR   HAMAP; MF_02120; LysA; 1; -.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01181; DAPDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Racem_decarbox_C; 1.
DR   TIGRFAMs; TIGR01048; lysA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Decarboxylase; Lyase;
KW   Lysine biosynthesis; Pyridoxal phosphate.
FT   REGION      268    271       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     227    227       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity).
FT   BINDING     271    271       Substrate (By similarity).
FT   BINDING     307    307       Substrate (By similarity).
FT   BINDING     311    311       Substrate (By similarity).
FT   BINDING     343    343       Substrate (By similarity).
FT   BINDING     378    378       Pyridoxal phosphate (By similarity).
FT   BINDING     378    378       Substrate (By similarity).
FT   MOD_RES      54     54       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   420 AA;  45777 MW;  8D022CAA18E5AD4C CRC64;
     MPRPLNSTDT DLTAENLLRL PAEFGCPVWV YDAQIIRRQI AQLGRFDVVR FAQKACSNIH
     ILRLMREQGV KVDSVSLGEI ERALAAGYAP QTHPDDIVFT ADVIDEATIA RVSELRIPVN
     AGSVDMLAQL GAVSPGHPVW LRVNPGFGHG HSQKTNTGGE NSKHGIWYSD LPAALAVIQR
     YGLNLIGIHM HIGSGVDYGH LEQVCGAMVR QVIDFGQDLQ AISAGGGLSI PYREGEEAID
     TDHYYGLWNA AREQIARHLG HPVKLEIEPG RFLVAEAGVL VSQVRSVKQM GSRHFVLIDA
     GFNDLMRPAM YGSYHHITAL AADGRDLTLA PLVETVVAGP LCESGDVFTQ QEGGKVETRA
     LPQVAPGDYL VLHDTGAYGA SMSSNYNSRP LLPEVLYDNG SARLIRRRQT IQELLALELC
//