ID Q0HN96_SHESM Unreviewed; 414 AA.
AC Q0HN96;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 01-MAY-2013, entry version 52.
DE RecName: Full=Diaminopimelate decarboxylase;
DE Short=DAP decarboxylase;
DE Short=DAPDC;
DE EC=4.1.1.20;
GN Name=lysA; OrderedLocusNames=Shewmr4_0391;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-2006) 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; CP000446; ABI37471.1; -; Genomic_DNA.
DR RefSeq; YP_732528.1; NC_008321.1.
DR ProteinModelPortal; Q0HN96; -.
DR STRING; 60480.Shewmr4_0391; -.
DR EnsemblBacteria; ABI37471; ABI37471; Shewmr4_0391.
DR GeneID; 4251724; -.
DR KEGG; she:Shewmr4_0391; -.
DR PATRIC; 23577210; VBISheSp133532_0406.
DR eggNOG; COG0019; -.
DR HOGENOM; HOG000045070; -.
DR KO; K01586; -.
DR OMA; AQVFDIV; -.
DR ProtClustDB; CLSK907584; -.
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; 45116 MW; D83990C0695C7A9E CRC64;
MDHFLYQDNT LYAEGCRVND LAQQYGTPLY IYSRATLERH WHAFNNAVAD HPHLVCYAVK
ANSNLAVLNV LARLGSGFDI VSGGELARVI EAGGDPAKVV FSGVGKTVAE MEQALNLGIY
CFNVESSAEL EQLNQVAGRL GKIAPVSLRV NPDVDAGTHP YISTGLKENK FGIAMDEAEV
VFARAHALPH LQVKGVDCHI GSQLTEIQPF LDAMDRMLAL IDRLAEQGIV IEHFDVGGGL
GVTYDDETPP HPDVYAAALL ARLGDRKLKL IFEPGRAIAA NAGIFVTQVL YLKENSDKRF
AIVDGAMNDL IRPALYSAWQ NIIPVNPRDE QAQVFDIVGP VCETGDFLGK DRALAIAAGD
LLVVRSSGAY GFAMASNYNT RPRAAEVMVD GDKAYLVRER EKLAQLWQGE QLLP
//
