ID Q0B594_BURCM Unreviewed; 450 AA.
AC Q0B594;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABI90679.1};
GN OrderedLocusNames=Bamb_5130 {ECO:0000313|EMBL:ABI90679.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI90679.1, ECO:0000313|Proteomes:UP000000662};
RN [1] {ECO:0000313|Proteomes:UP000000662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP000441; ABI90679.1; -; Genomic_DNA.
DR RefSeq; WP_011660062.1; NZ_CP009799.1.
DR AlphaFoldDB; Q0B594; -.
DR GeneID; 69548081; -.
DR KEGG; bam:Bamb_5130; -.
DR PATRIC; fig|339670.21.peg.5515; -.
DR eggNOG; COG0076; Bacteria.
DR Proteomes; UP000000662; Chromosome 2.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 285
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 450 AA; 47783 MW; CD8E5B4F3ED70DC3 CRC64;
MDELALLADA DRRAHAYLAA TNERRAYPDA AALAGLAAFD EPLPDTGRPA DDVLRLLDEH
GTTATVASNG PNYFGFVIGA TLPAAAAAER LMLAWDQCAS SFANSPVAAT IERQAARWIV
DVLGLPEGSA VGFGTSATAC TLVALVVARR ALLARKGWDV DEDGLIGAPE VKVVVSELVH
VTVKKALRVL GFGMKRVIVA PVDTHGRIDS AQLPPLDDMT ILCVQAGEVN TGEFDPFAAL
IPLAKAAGAW VHVDGAFGLW ARASSKRALT NGVDGADSWT TDGHKWLNTP YDAAMVICRD
AAALATAMNS DAVYLSGAQD AQKNLNLEFS RRARGIPVWA ALRALGRAGV ATMIERHCAQ
AARVADGLRV AGYDVLNRVV LNQVLVRAGT DDETTAILQA AQDSGDVWFG QTVWQGRPAF
RISVSSWRTE DQHIDRLVAL LTKLRGVHVG
//
