ID   Q62GA0_BURMA            Unreviewed;       423 AA.
AC   Q62GA0;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   09-FEB-2010, entry version 39.
DE   RecName: Full=Diaminopimelate decarboxylase;
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   -!- 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   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000010; AAU47904.1; -; Genomic_DNA.
DR   RefSeq; YP_104274.1; -.
DR   SMR; Q62GA0; 2-416.
DR   GeneID; 3091324; -.
DR   GenomeReviews; CP000010_GR; BMA2756.
DR   KEGG; bma:BMA2756; -.
DR   TIGR; BMA2756; -.
DR   HOGENOM; HBG672375; -.
DR   OMA; SIAGKCC; -.
DR   PhylomeDB; Q62GA0; -.
DR   BioCyc; BMAL243160:BMA_2756-MONOMER; -.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopime...; IEA:InterPro.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_decrbxlase.
DR   InterPro; IPR000183; De-COase2.
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   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.
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
//