DCDA_CAMJE
ID DCDA_CAMJE Reviewed; 402 AA.
AC Q9PII5; Q0PBJ5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=Cj0314;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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; AL111168; CAL34465.1; -; Genomic_DNA.
DR PIR; F81450; F81450.
DR RefSeq; WP_002858733.1; NC_002163.1.
DR RefSeq; YP_002343752.1; NC_002163.1.
DR AlphaFoldDB; Q9PII5; -.
DR SMR; Q9PII5; -.
DR IntAct; Q9PII5; 30.
DR STRING; 192222.Cj0314; -.
DR PaxDb; Q9PII5; -.
DR PRIDE; Q9PII5; -.
DR EnsemblBacteria; CAL34465; CAL34465; Cj0314.
DR GeneID; 904638; -.
DR KEGG; cje:Cj0314; -.
DR PATRIC; fig|192222.6.peg.306; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_0_7; -.
DR OMA; YCRSMAS; -.
DR UniPathway; UPA00034; UER00027.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
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; 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; 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..402
FT /note="Diaminopimelate decarboxylase"
FT /id="PRO_0000149919"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 224
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 259..262
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 356
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
FT MOD_RES 45
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02120"
SQ SEQUENCE 402 AA; 45375 MW; B133E3D798A3EE2E CRC64;
MDYKQLKQEF NTPFYIYNFD FIKERFLNLK EAFKARKSQI FYAVKANSNL SLLQMLANLD
SGFDCVSIGE VKRALKAGAK AYKIIFSGVG KTKEELRQAL EYDILYINLE SEAEMMLLES
VAKELNLKAR ISIRVNPNVD AKTHPYISTG LNENKFGVEI DIARKMYLYA KNSSFLEPVG
VHFHIGSQLL DISPIHEAAA IVAKLVRELK ALQIDLKFFD IGGGLGVAYE KNECEPDLYD
YAQGILAQLH GLDLTIGMEP GRYLVAKSGE FVCSVLYEKQ NKTKRFVVVD GAMNDLIRPS
LYEAYHEIIL PYNQGEESLC DVVGGICESG DFFAKARSLP STQSDDIMVI KNTGAYGFSM
SSNYNTRNKV CELALEEGQV RLIRQRENFE DQIALEEKFL KA
