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Database: UniProt/TrEMBL
Entry: F6CRK9_MARPP
LinkDB: F6CRK9_MARPP
Original site: F6CRK9_MARPP 
ID   F6CRK9_MARPP            Unreviewed;       417 AA.
AC   F6CRK9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   19-MAR-2014, entry version 17.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=Mar181_0716;
OS   Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Marinomonas.
OX   NCBI_TaxID=491952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181;
RX   PubMed=23458837; DOI=10.4056/sigs.2976373;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M.,
RA   Kyrpides N.C., Detter J.C., Copeland A., Lu M., Bruce D., Detter C.,
RA   Tapia R., Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of Marinomonas posidonica type strain (IVIA-
RT   Po-181(T)).";
RL   Stand. Genomic Sci. 7:31-43(2012).
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; CP002771; AEF53772.1; -; Genomic_DNA.
DR   RefSeq; YP_004480691.1; NC_015559.1.
DR   ProteinModelPortal; F6CRK9; -.
DR   EnsemblBacteria; AEF53772; AEF53772; Mar181_0716.
DR   GeneID; 10645543; -.
DR   KEGG; mpc:Mar181_0716; -.
DR   KO; K01586; -.
DR   BioCyc; MPOS491952:GI6N-742-MONOMER; -.
DR   UniPathway; UPA00034; UER00027.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-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; 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; SSF50621; 1.
DR   TIGRFAMs; TIGR01048; lysA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 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     345    345       Substrate (By similarity).
FT   BINDING     372    372       Pyridoxal phosphate (By similarity).
FT   BINDING     372    372       Substrate (By similarity).
FT   MOD_RES      60     60       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   417 AA;  45759 MW;  E0069234C137FDDF CRC64;
     MDLFAYSNQT LHAEGVALSD VAEQFGTPCY IYSRAMFERH YMDYAEAFAA HPTLICYAVK
     ACSNIAILNV LARLGAGFDI VSLGELERVL KAGGEPSKVM FSGLGKQEVE MRRALEVGIH
     CFNVESEAEL YRLDKVASEM GKKAPVSLRV NPDVDAKTHP YISTGLKENK FGIDIKEAVR
     IYQIANELPN LDVMGVDCHI GSQLTELQPF LDTFDRLVGL LDELAAVGIK IKHLDLGGGL
     GVRYRDEVPP KPADYAKLLL EKVKGMDVTL AFEPGRSIAA NAGVMLTQVE FLKCNDHKNF
     AIIDGAMNDL IRPSLYSAWM DIVPVSQQPT SEGKRVYDLV GPVCETGDFL GKDRELDIQA
     GDLLAVRSAG AYGFTMASNY NSRNRAAEVM VDGDTAYLIR ARETIEHQLA GEQVLPD
//
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