ID   D4ZCR4_SHEVD            Unreviewed;       414 AA.
AC   D4ZCR4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   01-MAY-2013, entry version 23.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=SVI_3838;
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 /
OS   DSS12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12;
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E.,
RA   Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M.,
RA   Kato C., Oshima T., Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella
RT   violacea, a psychrophilic and piezophilic bacterium from deep sea
RT   floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ03809.1; -; Genomic_DNA.
DR   RefSeq; YP_003558587.1; NC_014012.1.
DR   ProteinModelPortal; D4ZCR4; -.
DR   EnsemblBacteria; BAJ03809; BAJ03809; SVI_3838.
DR   GeneID; 8968294; -.
DR   KEGG; svo:SVI_3838; -.
DR   PATRIC; 35463858; VBISheVio92117_3685.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; GPICETS; -.
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      273    276       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     239    239       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity).
FT   BINDING     276    276       Substrate (By similarity).
FT   BINDING     312    312       Substrate (By similarity).
FT   BINDING     316    316       Substrate (By similarity).
FT   BINDING     343    343       Substrate (By similarity).
FT   BINDING     370    370       Pyridoxal phosphate (By similarity).
FT   BINDING     370    370       Substrate (By similarity).
FT   MOD_RES      60     60       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   414 AA;  45031 MW;  5F742B8B66614C0B CRC64;
     MDHFLYKNNE LLAEDCSVAD LARTHGTPLY IYSRATLERH WHAFDRAVAD HPHLICYAVK
     ANSNIAVLNV LARLGSGFDI VSGGELQRVI QAGGDPAKVV FSGVGKTAAE MEMALNLGIH
     CFNVESAAEL EQLNIVAGRI GKLAPVSLRI NPDVDAGTHP YISTGLKDNK FGIAMEQAEA
     IFARAAALPN LKVKGVDCHI GSQLTEIQPF LDAMDRMLAL IDRLAEQGIH IEHFDVGGGL
     GVPYDDETPP QPAVYAAALI ERLGDRKLKL IFEPGRAIAA NAGIFVTQVL YLKGNGDKHF
     ALVDGAMNDL IRPALYSAWQ NIIPVNPRDG ETLNYDIVGP VCETGDFLGK DRELNLAAGD
     FLAVRSSGAY GFTMSSNYNS RPRAAELMVD GEQAYVIRER EKVTQLWQGE QLLP
//