ID   Q1LR80_CUPMC            Unreviewed;       552 AA.
AC   Q1LR80;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABF07346.1};
DE            EC=4.1.1.- {ECO:0000313|EMBL:ABF07346.1};
GN   OrderedLocusNames=Rmet_0460 {ECO:0000313|EMBL:ABF07346.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF07346.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF07346.1; -; Genomic_DNA.
DR   RefSeq; WP_011515334.1; NC_007973.1.
DR   AlphaFoldDB; Q1LR80; -.
DR   STRING; 266264.Rmet_0460; -.
DR   KEGG; rme:Rmet_0460; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_4; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
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; IPR022517; Asp_decarboxylase_pyridox.
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   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         347
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   552 AA;  60005 MW;  1BA8376FFAFF156D CRC64;
     MKARKAGRSD NAREATGNDA EMGEGCPLHW FDADLGAFDD LERRVAEHPA DFFAGQDFDP
     VGACATREAS FASVQIPEDP TAPQQHADHL LNDVFRHVMP VASPTFVGHM TSSLPSFMPS
     LAKIVAALNQ NVVKLETSGA LTGLERQVIG MLHHLVFARD DAFYAQWLHN AEHSLGAFCS
     GGTTANLTAL WASRNNTLRA RDGFAGINQA GLVAALRHYG YAGLAIVVSE RGHYSLRKAA
     DILGIGRENL VPVGVDEDGR MRVDLLRDTL RDLQQRNIRT VAIVGIAGTT ETGAVDPLDA
     IADVAQEIGC HFHVDAAWGG ATLLSARERA RFAGIERADS VVIDAHKQFY VPMGAGMVLF
     RDPAWTQDII QHANYIVRKG SVDLGRHTLE GSRGSAAVML YANLHLLGRK GLAKLIDTGI
     DNAKYFASLI EQQPDFELDS RPQLCILTYR YVPAPVRAAL LSASPEQREQ LLEALDALTI
     NIQEMQRDAG RSFVSRTQLT SSQWGGRPIA VFRVVLANPD TTHEILQSLL EEQRGLAKQS
     PMLPALMAMV GG
//