ID   A6VGE0_METM7            Unreviewed;       436 AA.
AC   A6VGE0;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   01-MAY-2013, entry version 42.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=MmarC7_0447;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Sieprawska-Lupa M.,
RA   Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) 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; CP000745; ABR65516.1; -; Genomic_DNA.
DR   RefSeq; YP_001329667.1; NC_009637.1.
DR   ProteinModelPortal; A6VGE0; -.
DR   SMR; A6VGE0; 4-436.
DR   STRING; 426368.MmarC7_0447; -.
DR   EnsemblBacteria; ABR65516; ABR65516; MmarC7_0447.
DR   GeneID; 5328385; -.
DR   KEGG; mmz:MmarC7_0447; -.
DR   eggNOG; COG0019; -.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; HPKISTG; -.
DR   ProtClustDB; CLSK876448; -.
DR   BioCyc; MMAR426368:GHHL-494-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; 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      292    295       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     252    252       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity).
FT   BINDING     295    295       Substrate (By similarity).
FT   BINDING     331    331       Substrate (By similarity).
FT   BINDING     335    335       Substrate (By similarity).
FT   BINDING     361    361       Substrate (By similarity).
FT   BINDING     389    389       Pyridoxal phosphate (By similarity).
FT   BINDING     389    389       Substrate (By similarity).
FT   MOD_RES      71     71       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   436 AA;  48078 MW;  96972A43D2BA26EE CRC64;
     MEFLGNEMLT VEGKNLKIDG YDASELAKTY GTPLYVMSET QTVKNFTRYV DSFKEYSEKT
     GKEFIISFAY KANTNLAVTK LLSKLGCGAD IVSAGELYIA KLSNVPSEKI VFNGNCKLKE
     EIKMGIEAEI RAFNVDSISE LVLINETAKE MGKIANVAFR VNPNVDAKTH PKISTGMKKN
     KFGLDIESGI ALETIKMAEK MENVKIVGIH CHIGSQLTYI SPFVEEARKI MDFVVSLKNE
     GIEIKDVNLG GGLGIPYDKN TKIPVQKDLS KAVLDVIYEY EGKIELPNLI LEPGRSLVAT
     AGVLLGTVEH VKETPVAKWI MIDAGMNDMM RPAIYEAYHE IVPCTIRDEK EVVSVAGGLC
     ESSDVFGKDR ELSKMEVKDT VAILDVGAYG ISMANNYNSR GKPAMILTNE KEVSLIRVRE
     TLADLISKDI VPNHLL
//