ID   DCDA_BACMT              Reviewed;         432 AA.
AC   P41023;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Bacillus methanolicus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MGA3;
RX   PubMed=8215365; DOI=10.1128/aem.59.9.2927-2937.1993;
RA   Mills D.A., Flickinger M.C.;
RT   "Cloning and sequence analysis of the meso-diaminopimelate decarboxylase
RT   gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase
RT   genes.";
RL   Appl. Environ. Microbiol. 59:2927-2937(1993).
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; L18879; AAC36985.1; -; Unassigned_DNA.
DR   PIR; I39877; I39877.
DR   AlphaFoldDB; P41023; -.
DR   SMR; P41023; -.
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..432
FT                   /note="Diaminopimelate decarboxylase"
FT                   /id="PRO_0000149914"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         248
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         290..293
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         390
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   BINDING         390
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT   MOD_RES         66
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
SQ   SEQUENCE   432 AA;  47821 MW;  8EEABA7E12E2B49D CRC64;
     MYFHGTTKVN EKGHLEIGGV DTIELAQKYG TPLYVYDVAL IRERARGFKN TFDELGIKAQ
     VAYASKAFST VAMIQLAEEE GLSLDVVSGG ELYTALVAGF PVHKIHFHGN NKSRAELEMA
     LEHQIGCIVV DNFHELDLID SICSEKNVKT NILLRVTPGI EAHTHDYILT GQEDSKFGFD
     LQNGQAEKAL QIALNSNFVE VLGVHCHIGS QIFDTTGFVL AARKIFEKLK EWKDRLSYEP
     KVLNLGGGFG IRYTEEDDPI PASQYVKEII NEVKKQVSAY SMKMPEIWIE PGRSLVGDAG
     TTLYQIGSRK DVPNVRHYVA VDGGMSDNIR PALYNAKYEA VLANKPLAKA DETVSIAGKC
     CESGDMLIWD LPLPKADSDD ILAVFCTGAY GYSMANNYNR IPRPAVVFVE NGESMLVVKR
     KHMRTSSAMI CL