ID A0A0J1DJG4_9FIRM Unreviewed; 416 AA.
AC A0A0J1DJG4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KLU39135.1};
GN ORFNames=AA931_11145 {ECO:0000313|EMBL:KLU39135.1};
OS Peptococcaceae bacterium 1109.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1655638 {ECO:0000313|EMBL:KLU39135.1, ECO:0000313|Proteomes:UP000036486};
RN [1] {ECO:0000313|EMBL:KLU39135.1, ECO:0000313|Proteomes:UP000036486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1109 {ECO:0000313|EMBL:KLU39135.1};
RA Town J.R., Dumonceaux T.J.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU39135.1}.
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DR EMBL; LDJB01000004; KLU39135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1DJG4; -.
DR STRING; 1655638.AA931_11145; -.
DR PATRIC; fig|1655638.3.peg.2249; -.
DR Proteomes; UP000036486; 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 29..276
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 279..367
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 340
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 416 AA; 46422 MW; 7B71FEEE44DE2FC9 CRC64;
MKRPFVSAEQ LRHIVEEHPT PFHLYDEAGI RKNARRLNKA FAWNPGFREY FAVKATPNPR
ILQILQEEGC GVDCATLTEL LLAEAVGFSG REMMFSSNMT PFQDFAYAYG LGAILNLDDI
SDIDYLERLP NIPELVCCRY NPGGDFSLSN EIMDTPGEAK YGFTREQLTT GYRRLMDLGV
RKFGLHAFLA SNTTNSEYYP VLARLLFETA VELHKETGAE ISLINLSGGI GIPYRPHEQP
VDIEAVGEGV RQAYAEVLAP AGLENVAIAA ELGRYMLGPY GCLVATAIRQ KETYKHYIGL
DACAANLMRP AMYRAYHHIT VAGKEDWPCD HVYDVVGGLC ENNDKFAIDR PLPRIELGDL
VVIHDTGAHG FSMGYNYNGK LRSAELLLRA DGSVELIRRA ETPADYFATL ELPIRK
//
