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Database: UniProt
Entry: T0UV86_LACLC
LinkDB: T0UV86_LACLC
Original site: T0UV86_LACLC 
ID   T0UV86_LACLC            Unreviewed;       419 AA.
AC   T0UV86;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:EQC87612.1};
GN   ORFNames=LLT1_09675 {ECO:0000313|EMBL:EQC87612.1};
OS   Lactococcus cremoris subsp. cremoris TIFN1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=1234871 {ECO:0000313|EMBL:EQC87612.1, ECO:0000313|Proteomes:UP000015849};
RN   [1] {ECO:0000313|EMBL:EQC87612.1, ECO:0000313|Proteomes:UP000015849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIFN1 {ECO:0000313|EMBL:EQC87612.1};
RX   PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA   Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA   van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA   Kleerebezem M., Smid E.J.;
RT   "Multifactorial diversity sustains microbial community stability.";
RL   ISME J. 7:2126-2136(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|RuleBase:RU003737}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC87612.1}.
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DR   EMBL; ASXF01000111; EQC87612.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0UV86; -.
DR   PATRIC; fig|1234871.3.peg.947; -.
DR   Proteomes; UP000015849; Unassembled WGS sequence.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
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; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          30..279
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          281..369
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        342
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         54
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   419 AA;  47247 MW;  BBC1CDA1C2FBB530 CRC64;
     MKTPFVTKEQ LEQITAEYPT PFHLYDEKGI RQKARDLHKA FAWNKGFKEF FAVKATPTPA
     ILKILHEEGC GVDCASYIEL LLSEKCGFDG TEMMFSSNDT PAEEFQFANQ LGATINLDAY
     EHIEFLKNLP DFVFPKTMSL RYNPGGVFAM GTKIMDNPEE SKFGMTKAQL IQGIKDLQKL
     GVKEFGMHSF LASNTVTNDY YPELARKLFE LELEIRQETG VTLDFINLSG GIGVNYRPDE
     EANDIAKIGQ GVHKAYEEVL TANGIENLKI YTELGRFMLA PHGHLITKVL HLKETYRKYV
     GVDASAVNLM RPAFYDAYHH ITVAGKEKQE ATETYDITGS LCENNDKFAK ERAFPEIKVG
     DLLVIHDTGA HGFSMGYQYN AKLRSAEILL QEDGKTRLIC RAENPADYFA TLDGFDFNN
//
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