ID A0A0J1CJH1_9BURK Unreviewed; 402 AA.
AC A0A0J1CJH1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KLU20571.1};
GN ORFNames=EOS_40710 {ECO:0000313|EMBL:KLU20571.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU20571.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU20571.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU20571.1}.
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DR EMBL; AEJF01000249; KLU20571.1; -; Genomic_DNA.
DR RefSeq; WP_047897906.1; NZ_AEJF01000249.1.
DR AlphaFoldDB; A0A0J1CJH1; -.
DR PATRIC; fig|908627.4.peg.9140; -.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000035963; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
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; 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; 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}.
FT DOMAIN 31..380
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 39..284
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 61
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 402 AA; 43217 MW; A3CDD9871879C636 CRC64;
MTHPFSVQAG VLQIGGVDLR RLAARAGHTP FYVYDRSLVD ARIRALRQTL PHGIELHYSI
KANPMPAMVH HLAARLDGFD VASAGEMMLA LDAGTRPERI GFAGPGKSHD ELRRAVAAGV
VIHIESATQL RLVTALGWEF GVRPCVAIRV NPDFQIGKGG MRMGGGAAPF GVDASLVPAL
LLELARQEVA FAGFHVFWGS QCLHAPTIIQ AHRQSAELVM RLADNLEVPP AFINLGGGFG
IPYFPGEDPL DFDAVGEAMH DWLPGLHRRL PGTRVVLELG RYLVGEAGIY VCRVVDRKVS
CGETFLITDG GLHHHLAASG NFGQVLRRNY PVLIGNRLDE PAQERSHVVG CLCTPLDRIA
DGAHLPATSI GDLVVVLQSG AYGRSASPTD FLAHPPPAEM LV
//
