ID F6CRK9_MARPP Unreviewed; 417 AA.
AC F6CRK9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 03-APR-2013, entry version 13.
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;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Lucas-Elio P., Johnston A.,
RA Sanchez-Amat A., Woyke T.;
RT "Complete sequence of Marinomonas posidonica IVIA-Po-181.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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 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: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; 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.
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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