DCDA_MYCTO
ID DCDA_MYCTO Reviewed; 447 AA.
AC P9WIU6; L0T7U9; P0A5M4; P31848;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Diaminopimelate decarboxylase;
DE Short=DAP decarboxylase;
DE Short=DAPDC;
DE EC=4.1.1.20;
GN Name=lysA; OrderedLocusNames=MT1332;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC diaminopimelate (meso-DAP) to L-lysine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
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; disulfide-linked. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC LysA subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK45594.1; -; Genomic_DNA.
DR PIR; A70773; A70773.
DR RefSeq; WP_003406632.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIU6; -.
DR SMR; P9WIU6; -.
DR EnsemblBacteria; AAK45594; AAK45594; MT1332.
DR GeneID; 45425267; -.
DR KEGG; mtc:MT1332; -.
DR PATRIC; fig|83331.31.peg.1438; -.
DR HOGENOM; CLU_026444_0_1_11; -.
DR UniPathway; UPA00034; UER00027.
DR Proteomes; UP000001020; 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; 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; 2.
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; Disulfide bond; Lyase;
KW Lysine biosynthesis; Pyridoxal phosphate.
FT CHAIN 1..447
FT /note="Diaminopimelate decarboxylase"
FT /id="PRO_0000427943"
FT ACT_SITE 375
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 300..303
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT DISULFID 93
FT /note="Interchain (with C-375)"
FT /evidence="ECO:0000250"
FT DISULFID 375
FT /note="Interchain (with C-72)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 47458 MW; 3CE085A33F7F30F4 CRC64;
MNELLHLAPN VWPRNTTRDE VGVVCIAGIP LTQLAQEYGT PLFVIDEDDF RSRCRETAAA
FGSGANVHYA AKAFLCSEVA RWISEEGLCL DVCTGGELAV ALHASFPPER ITLHGNNKSV
SELTAAVKAG VGHIVVDSMT EIERLDAIAG EAGIVQDVLV RLTVGVEAHT HEFISTAHED
QKFGLSVASG AAMAAVRRVF ATDHLRLVGL HSHIGSQIFD VDGFELAAHR VIGLLRDVVG
EFGPEKTAQI ATVDLGGGLG ISYLPSDDPP PIAELAAKLG TIVSDESTAV GLPTPKLVVE
PGRAIAGPGT ITLYEVGTVK DVDVSATAHR RYVSVDGGMS DNIRTALYGA QYDVRLVSRV
SDAPPVPARL VGKHCESGDI IVRDTWVPDD IRPGDLVAVA ATGAYCYSLS SRYNMVGRPA
VVAVHAGNAR LVLRRETVDD LLSLEVR
