ID   Q62GA0_BURMA            Unreviewed;       423 AA.
AC   Q62GA0;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   14-DEC-2011, entry version 50.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=BMA2756;
OS   Burkholderia mallei (Pseudomonas mallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=13373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA   Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA   Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA   Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA   Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily.
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DR   EMBL; CP000010; AAU47904.1; -; Genomic_DNA.
DR   RefSeq; YP_104274.1; NC_006348.1.
DR   ProteinModelPortal; Q62GA0; -.
DR   GeneID; 3091324; -.
DR   GenomeReviews; CP000010_GR; BMA2756.
DR   KEGG; bma:BMA2756; -.
DR   PATRIC; 19120663; VBIBurMal55007_2825.
DR   TIGR; BMA2756; -.
DR   HOGENOM; HBG672375; -.
DR   OMA; DAHTHPY; -.
DR   PhylomeDB; Q62GA0; -.
DR   ProtClustDB; CLSK897530; -.
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   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; IPR000183; Orn/DAP/Arg_de-COase.
DR   Gene3D; G3DSA:2.40.37.10; Ala_racemase/Decarboxylase_C; 1.
DR   KO; K01586; -.
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; 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      278    281       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     241    241       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity).
FT   BINDING     281    281       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
FT   BINDING     321    321       Substrate (By similarity).
FT   BINDING     349    349       Substrate (By similarity).
FT   BINDING     376    376       Pyridoxal phosphate (By similarity).
FT   BINDING     376    376       Substrate (By similarity).
FT   MOD_RES      62     62       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   423 AA;  45221 MW;  C8B498609408D298 CRC64;
     MTQAAFDYVD GTLHAERVST VELAERFGTP LFVYSRAALT AAYEAYAKAC AGRRASIHVA
     VKANSNLGVL NVFARLGAGF DIVSGGELAR VLAAGGRARD VVFSGVGKSA DEMRVALEAG
     VKCFNVESIP ELDRLNAVAA SLGKRAPVSL RVNPDVDPKT HPYISTGLKA NKFGIAFDDA
     RATYRAAAAL PNLEVVGIDC HIGSQITELS PYLDAIDKLL DLVERIEADG VQIHHVDVGG
     GLGITYDDET PPDIGAYVRA VLARIDARGH GQREIWFEPG RSLTGNAGIL LTRVEFLKQG
     EEKNFAIVDA AMNDLARPAM YQAFHAIVPV APRTDVAAAV YDIVGPVCES GDWLGRERSL
     AIAPGDLLAI RSAGAYGFTM SSNYNTRPRA AEVIVDGANA HLVRPRETVE SLFEHETILP
     EGR
//