ID   A0A285ZTR6_9SPHI        Unreviewed;       385 AA.
AC   A0A285ZTR6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|RuleBase:RU003738};
DE            EC=4.1.1.20 {ECO:0000256|RuleBase:RU003738};
GN   ORFNames=SAMN06297358_0968 {ECO:0000313|EMBL:SOD13022.1};
OS   Pedobacter xixiisoli.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD13022.1, ECO:0000313|Proteomes:UP000219281};
RN   [1] {ECO:0000313|EMBL:SOD13022.1, ECO:0000313|Proteomes:UP000219281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD13022.1,
RC   ECO:0000313|Proteomes:UP000219281};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU003738};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50, ECO:0000256|RuleBase:RU003738};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|RuleBase:RU003738}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|RuleBase:RU003737}.
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DR   EMBL; OCMT01000001; SOD13022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285ZTR6; -.
DR   OrthoDB; 9802241at2; -.
DR   UniPathway; UPA00034; UER00027.
DR   Proteomes; UP000219281; Unassembled WGS sequence.
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; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR01048; lysA; 1.
DR   PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003738};
KW   Decarboxylase {ECO:0000256|RuleBase:RU003738};
KW   Lyase {ECO:0000256|RuleBase:RU003738};
KW   Lysine biosynthesis {ECO:0000256|RuleBase:RU003738};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          18..361
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   DOMAIN          33..270
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   ACT_SITE        334
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   385 AA;  42964 MW;  1A3DDEADC5D2DDEA CRC64;
     MFSDKDIAHF SNLETPFYYY DLNLLRETLK VCSEAANAYN FHVHYAMKAN FNDKVLAQIK
     QAGFGADAVS GGEVKKAIES GFANNKVVFA GVGKSDREIN YALDQDIFCF NVESLQELQV
     INELAEKKGK VAKVAIRINP NVDAHTHANI TTGLDENKFG INSWDMPACA DILSVSANLE
     FVGIHFHIGS QITNLDVYKN LCVRVNEFAA WFEDKNFKVK VLNVGGGLGI DYHNPNAQIP
     NFEAYFKIFA DFLDIKPHQE VHFELGRALV GQSSSLISRV LYVKNGKKKN FIVLDAGMTE
     LMRPALYQAY HQIENISPKT TETTVKYDVV GPICESTDCF GKEVALQETF RNDLIAIRST
     GAYGEVMASN YNLRDAIVTV TSEDY
//