ID A0A257FR08_9BURK Unreviewed; 421 AA.
AC A0A257FR08;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pyridoxal-dependent decarboxylase, exosortase A system-associated {ECO:0000313|EMBL:OYU28536.1};
GN ORFNames=CFE41_05865 {ECO:0000313|EMBL:OYU28536.1};
OS Burkholderiales bacterium PBB2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015564 {ECO:0000313|EMBL:OYU28536.1, ECO:0000313|Proteomes:UP000215624};
RN [1] {ECO:0000313|EMBL:OYU28536.1, ECO:0000313|Proteomes:UP000215624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB2 {ECO:0000313|EMBL:OYU28536.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU28536.1}.
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DR EMBL; NKIM01000006; OYU28536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257FR08; -.
DR Proteomes; UP000215624; 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; cd06839; PLPDE_III_Btrk_like; 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; IPR017530; DCO2ase_PEP1.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR03099; dCO2ase_PEP1; 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; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000215624}.
FT DOMAIN 47..399
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 55..300
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 372
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 77
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 421 AA; 44659 MW; 9F312593CF26D7BD CRC64;
MSDATPTPKR APVHAPMSQF PQAADGSLQI GGQSLSLLAE RVGQTPFYAY DRGLLRDRVA
QLRAALPKQV KLHYAMKANP LPAVVGWMAG LVDGIDVASA GELQVALNAG ADPVEISFAG
PGKRDIELHQ AVAAGVLVNV ESARELPVLA AASKRYGLPA RVAVRVNPDF ELKGSGMKMG
GGPKQFGIDT EQMPELLAEI GRLGLAFEGF HLFAGSQNLK PESICEAQQK SYELALRLAA
LAPSPVKFLN LGGGFGITYF PGEHALDLAP IGANLQQLVE RAAVEMPQAH LVIELGRYLV
GEAGIYVTRI VDRKVSRGQT YLVTDGGLNH HLSASGNFGQ VIRKNYPVTI VRQHGATPVA
EREIASVVGP LCTPLDLLAD RMDLPVAEIG DLAVVFQSGA YGASASPEHF LGHPRCVEVL
V
//
