ID B8E691_SHEB2 Unreviewed; 414 AA.
AC B8E691;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 35.
DE RecName: Full=Diaminopimelate decarboxylase;
DE Short=DAP decarboxylase;
DE Short=DAPDC;
DE EC=4.1.1.20;
GN Name=lysA; OrderedLocusNames=Sbal223_3897;
OS Shewanella baltica (strain OS223).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J.,
RA Konstantinidis K., Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001252; ACK48372.1; -; Genomic_DNA.
DR RefSeq; YP_002359795.1; NC_011663.1.
DR ProteinModelPortal; B8E691; -.
DR STRING; 407976.Sbal223_3897; -.
DR EnsemblBacteria; ACK48372; ACK48372; Sbal223_3897.
DR GeneID; 7086660; -.
DR KEGG; sbp:Sbal223_3897; -.
DR PATRIC; 23484222; VBISheBal125792_4028.
DR eggNOG; COG0019; -.
DR HOGENOM; HOG000045070; -.
DR KO; K01586; -.
DR OMA; GPICETS; -.
DR ProtClustDB; CLSK907584; -.
DR BioCyc; SBAL407976:GJ6Y-4012-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 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; 44969 MW; C86D6C8D40325D8C CRC64;
MDHFLYQQNA LHAEGCQVAD LAQTYGTPLY IYSRATLERH WHAFNNAVAD HPHLICYAVK
ANANLAVLNV LARLGSGFDI VSGGELARVM EAGGDPAKVV FSGVGKTAAE MEQALNLGIY
CFNVESSAEL EQLNLVAGRL GKVAPVSLRI NPDVDAGTHP YISTGLKENK FGIAMDEAEI
VFARAHALPH LKVKGVDCHI GSQLTEIKPF LDAMDRMLAL IDRLAEQGIV IEHFDVGGGL
GVTYDAETPP HPDVYAAAIL ARLGDRQLKL IFEPGRAIAA NAGIFVTQVL YLKENSDKRF
AIVDGAMNDL IRPALYSAWQ NIIPVVPRDS EAYEFDIVGP VCETGDFLGK NRQLALAAGD
LLAVRSSGAY GFAMASNYNT RPRAAEVMVD GEQAFLVRER EKLSQLWQGE QLLP
//
