ID DCDA_STRCO Reviewed; 440 AA.
AC Q9ZBH5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 15-MAR-2017, entry version 107.
DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120};
DE Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120};
DE Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120};
DE EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120};
GN Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120};
GN OrderedLocusNames=SCO6438; ORFNames=SC9B5.05;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces
RT coelicolor A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP-
CC Rule:MF_02120}.
CC -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine +
CC CO(2). {ECO:0000255|HAMAP-Rule:MF_02120}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02120};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02120}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02120}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC family. LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}.
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DR EMBL; AL939127; CAA22747.1; -; Genomic_DNA.
DR PIR; T35925; T35925.
DR RefSeq; NP_630523.1; NC_003888.3.
DR RefSeq; WP_011030919.1; NC_003888.3.
DR ProteinModelPortal; Q9ZBH5; -.
DR SMR; Q9ZBH5; -.
DR STRING; 100226.SCO6438; -.
DR EnsemblBacteria; CAA22747; CAA22747; CAA22747.
DR GeneID; 1101877; -.
DR KEGG; sco:SCO6438; -.
DR PATRIC; 23742783; VBIStrCoe124346_6538.
DR eggNOG; ENOG4107TFS; Bacteria.
DR eggNOG; COG0019; LUCA.
DR HOGENOM; HOG000045070; -.
DR InParanoid; Q9ZBH5; -.
DR KO; K01586; -.
DR OMA; NISVGHI; -.
DR OrthoDB; POG091H013X; -.
DR PhylomeDB; Q9ZBH5; -.
DR UniPathway; UPA00034; UER00027.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd06828; PLPDE_III_DapDC; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 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 InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43727:SF3; PTHR43727:SF3; 1.
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; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 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; Reference proteome.
FT CHAIN 1 440 Diaminopimelate decarboxylase.
FT /FTId=PRO_0000149935.
FT REGION 275 278 Pyridoxal phosphate binding.
FT {ECO:0000255|HAMAP-Rule:MF_02120}.
FT ACT_SITE 348 348 Proton donor. {ECO:0000255}.
FT BINDING 234 234 Pyridoxal phosphate; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_02120}.
FT BINDING 278 278 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_02120}.
FT BINDING 314 314 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_02120}.
FT BINDING 318 318 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_02120}.
FT BINDING 349 349 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_02120}.
FT BINDING 384 384 Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT Rule:MF_02120}.
FT BINDING 384 384 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_02120}.
FT MOD_RES 61 61 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000255|HAMAP-Rule:MF_02120}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 21 425 ihamap:LysA [T]
FT MYHIT 55 282 ipfam:Orn_Arg_deC_N [T]
FT MYHIT 222 236 ipat:ODR_DC_2_2 [T]
FT MYHIT 58 76 ipat:ODR_DC_2_1 [T]
FT MYHIT 239 382 ipfam:Orn_DAP_Arg_deC [T]
SQ SEQUENCE 440 AA; 47549 MW; 8DC03E8650DB3921 CRC64;
MTSPSAPSSA ERPRLPGALD GPRLAAAAAE HGTPLWLYDA ATIRAQIDRL RRFDVIRYAQ
KACSNLHILR LMREEGVHVD AVSEGEIERA LAAGYRVGGD DEPIVFTADL LNRSTLRRVV
ELGIPVNAGS PQMLDQVGRA APGHPVWIRI NPGFGHGHSR KTNTGGEHSK HGIWHEHLEE
SLALVDRHGL DLVGLHMHIG SGVDYGHLES VCETMVKQVR MAGRDIRAIS AGGGLSVPYT
PGDPEIDTDR YFELWDAARR ELVSELGHPV RLEIEPGRFL VAGAGVLAAE VRAQKPVGSN
YFVLVDAGFN DLMRPAMYGS NHRVSVLDAD GAPRASDARD TVLAGPLCES GDVFTQVEGG
DVEPVPVPRT DVGDLVVFHD TGAYGASMSS TYNSRPLIPE VLVDGAETRL IRRRQTVAEL
LAPELEPGPA LSPRPSRDPR
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