DCDA_PSEAE
ID DCDA_PSEAE Reviewed; 415 AA.
AC P19572;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
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}; OrderedLocusNames=PA5277;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3143046; DOI=10.1093/oxfordjournals.molbev.a040515;
RA Martin C., Cami B., Yeh P., Stragier P., Parsot C., Patte J.-C.;
RT "Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary
RT relationship with other amino acid decarboxylases.";
RL Mol. Biol. Evol. 5:549-559(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:
CC Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine;
CC Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC Evidence={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 family.
CC LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}.
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DR EMBL; M23174; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; AE004091; AAG08662.1; -; Genomic_DNA.
DR PIR; A31133; A31133.
DR PIR; F82986; F82986.
DR RefSeq; NP_253964.1; NC_002516.2.
DR RefSeq; WP_003114343.1; NZ_QZGE01000020.1.
DR AlphaFoldDB; P19572; -.
DR SMR; P19572; -.
DR STRING; 287.DR97_2648; -.
DR PaxDb; P19572; -.
DR PRIDE; P19572; -.
DR DNASU; 877749; -.
DR EnsemblBacteria; AAG08662; AAG08662; PA5277.
DR GeneID; 877749; -.
DR KEGG; pae:PA5277; -.
DR PATRIC; fig|208964.12.peg.5531; -.
DR PseudoCAP; PA5277; -.
DR HOGENOM; CLU_026444_0_0_6; -.
DR InParanoid; P19572; -.
DR OMA; YCRSMAS; -.
DR PhylomeDB; P19572; -.
DR BioCyc; PAER208964:G1FZ6-5398-MON; -.
DR UniPathway; UPA00034; UER00027.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IMP:PseudoCAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
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; 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 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; Decarboxylase; Lyase; Lysine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..415
FT /note="Diaminopimelate decarboxylase"
FT /id="PRO_0000149933"
FT ACT_SITE 342
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 273..276
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 370
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT MOD_RES 60
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT CONFLICT 392
FT /note="E -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="Q -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45491 MW; 11516BC23547C7D5 CRC64;
MDTFSYRDAE LFAEGVALSR IAERFGTPTY VYSRAHIEAQ YRAYADALAG MPHLVCFAVK
ANSNLGVLNV LARLGAGFDI VSRGELERVL AAGGDPAKVV FSGVGKTRDD MRRALEVGVH
CFNVESGEEL ERLQRVAAEL GVKAPVSLRV NPDVDAQTHP YISTGLKENK FGIAIDEAEA
VYARAAELDH LEVIGVDCHI GSQLTQLEPF LDALERLLGL VDRLAGKGIG IRHLDLGGGL
GVRYRDEQPP LAGDYIRAIR ERLHGRDLTL VFEPGRSIVA NAGVLLTRVE YLKHTEHKDF
AIVDAAMNDL IRPALYQAWM DVQAVRPRDA APRRYDLVGP ICETGDFLAK DRDLALAEGD
LLAVRSAGAY GFVMSSNYNT RGRAAEVLVD GEQTHEVRRR ETVQELYAGE SLLPQ
