ID E4PK80_MARAH Unreviewed; 416 AA.
AC E4PK80;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 01-MAY-2013, entry version 18.
DE RecName: Full=Diaminopimelate decarboxylase;
DE Short=DAP decarboxylase;
DE Short=DAPDC;
DE EC=4.1.1.20;
GN Name=lysA; OrderedLocusNames=HP15_247;
OS Marinobacter adhaerens (strain HP15).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Marinobacter.
OX NCBI_TaxID=225937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HP15;
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H.,
RA Yarza P., Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain
RT (HP15).";
RL Submitted (FEB-2010) 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; CP001978; ADP96011.1; -; Genomic_DNA.
DR RefSeq; YP_005883939.1; NC_017506.1.
DR ProteinModelPortal; E4PK80; -.
DR EnsemblBacteria; ADP96011; ADP96011; HP15_247.
DR GeneID; 12400293; -.
DR KEGG; mad:HP15_247; -.
DR PATRIC; 43112588; VBIMarBac104501_0240.
DR KO; K01586; -.
DR OMA; QGIDCHI; -.
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 344 344 Substrate (By similarity).
FT BINDING 371 371 Pyridoxal phosphate (By similarity).
FT BINDING 371 371 Substrate (By similarity).
FT MOD_RES 60 60 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 416 AA; 45646 MW; 4736A19E6080AE93 CRC64;
MDHFNYRDGE LYAEDIPVSA IADRFGTPAY VYSRATLERH YRAYDDALRD HPHLVCYAVK
ANSNLAVLNV LARLGAGFDI VSAGELERVL RAGGDPSRVV FSGVGKQEWE MKRALEVGVR
CFNVESDTEL DRLNAVAGEL GVKAPISLRV NPDVDAGTHP YISTGLKENK FGIDIAEASQ
VYARAAGMPN LDVKGVDCHI GSQLTSVSPF LDALDRVLAL IDSLADQGIH IHHLDMGGGL
GVTYNQEQPP QPSDYVKALA ERLGDRKLEL ILEPGRSIAA NAGILVTRVE FLKCTEHRNF
AIIDAAMNDL IRPALYSAWQ AIIPVKPHQD GEEKAWDLVG PVCETGDFLG KDRHLRLQAG
DLLAVRSAGA YGFVMSSNYN TRNRPPELMV DGDQVHVVRR RETLEDQLAP ESCLPE
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