ID   DCDA_PSEFL              Reviewed;         416 AA.
AC   O05321;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120};
DE            Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120};
GN   Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120};
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCS365;
RX   PubMed=9618537; DOI=10.1073/pnas.95.12.7051;
RA   Dekkers L.C., Phoelich C.C., van der Fits L., Lugtenberg B.J.J.;
RT   "A site-specific recombinase is required for competitive root colonization
RT   by Pseudomonas fluorescens WCS365.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:7051-7056(1998).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine;
CC         Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02120};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02120};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}.
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DR   EMBL; Y12268; CAA72943.1; -; Genomic_DNA.
DR   PIR; T10458; T10458.
DR   AlphaFoldDB; O05321; -.
DR   SMR; O05321; -.
DR   STRING; 690597.JH730915_gene4360; -.
DR   PRIDE; O05321; -.
DR   eggNOG; COG0019; Bacteria.
DR   UniPathway; UPA00034; UER00027.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   InterPro; IPR029066; PLP-binding_barrel.
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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 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; Decarboxylase; Lyase; Lysine biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN           1..416
FT                   /note="Diaminopimelate decarboxylase"
FT                   /id="PRO_0000149934"
FT   ACT_SITE        343
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         240
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         274..277
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         371
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   MOD_RES         60
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
SQ   SEQUENCE   416 AA;  45222 MW;  088F26E723062D56 CRC64;
     MDAFNYRGGE LFAEGVALSA IAERFGTPTY VYSRAHIEAQ YRTFADALEG MPHLVCFAVK
     ANSNLGVLNV LARLGAGFDI VSGGELERVL AAGGSADKIV FSGVGKTRED MRRALEVGVH
     CFNIESTDEL GSRLQIVAAE LGVRAPISLR VNPDVDAGTH PYISTGLKEN KFGIAIADAE
     DVYVRAAQLP NLEVLGVDCH IGSQLTTLEP FIDALDRLLA LVDRLGDCGI YLRHIDLGGG
     VGVRYRDEEP PLVADYIKAV RERLDGRDLA LMFEPGRYIV ANAGVLLTQV EYLKHTEHKD
     FAIVDAAMND LIRPALYQAW MDVTAVRPRD TAARSYDIVG PICETGDFLA KGRELALEEG
     DLLAVHSAGA YGFVMSSNYN TRGRCAEVLV DGDQAFEVRR RETVAELFAG ESLLPE