ID A0A0K1F6J1_9ACTN Unreviewed; 443 AA.
AC A0A0K1F6J1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:AKT50030.1};
GN ORFNames=ADJ70_10670 {ECO:0000313|EMBL:AKT50030.1};
OS Olsenella sp. oral taxon 807.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=712411 {ECO:0000313|EMBL:AKT50030.1, ECO:0000313|Proteomes:UP000059853};
RN [1] {ECO:0000313|Proteomes:UP000059853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0089 {ECO:0000313|Proteomes:UP000059853};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-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}.
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DR EMBL; CP012069; AKT50030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1F6J1; -.
DR STRING; 712411.ADJ70_10670; -.
DR KEGG; olo:ADJ70_10670; -.
DR PATRIC; fig|712411.3.peg.852; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000059853; Chromosome.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 24..374
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 32..284
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 347
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 443 AA; 48665 MW; 04CE28CB89EF839B CRC64;
MSQKRPFITA DRLEAIASRY PTPFYLYDER GIRENARRVL EAFAWNPGFR EYFAVKATPN
PALIDILRDC GCGVDCSSEC ELMLAEAMGM LGDDIMFSSN DTPAQEFERA LALGATINLD
DITHVAMLDE AVRSVGVDYP HTVSLRLNPG GDFAFANGIF GSPEGAKFGL TEPQALEAAR
LLAKRGVEHL GLHAMLASNT VTNGYYPALA RTLFATAITL ERELGVDVSL VNLSGGVGVA
YEPDERENDI ALIGELVRQV YEERLVPVGM GDVRIATELG RYMLAPFGAL VTRVIHSKET
YHHYLGVDAC AANLMRPMLY GAYHHITVMG KEDASACRRY DVVGMLCENS DRLATDRPLP
EVEVGDLLFV HDVGAHGHSM GYNYNGRLRS AELLLREDGE VELIRRAETP ADYFATLDVL
PVGRRLLKRA GGQGPARRKS ARP
//
