ID   Q471E3_CUPPJ            Unreviewed;       552 AA.
AC   Q471E3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:AAZ60990.1};
GN   OrderedLocusNames=Reut_A1624 {ECO:0000313|EMBL:AAZ60990.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ60990.1};
RN   [1] {ECO:0000313|EMBL:AAZ60990.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ60990.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) 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; CP000090; AAZ60990.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q471E3; -.
DR   STRING; 264198.Reut_A1624; -.
DR   KEGG; reu:Reut_A1624; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_4; -.
DR   OrthoDB; 9803665at2; -.
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}.
FT   MOD_RES         341
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   552 AA;  60027 MW;  25B649BD8D15A2C9 CRC64;
     MTPDTSLEKT SQSTDGGDDC PLRWFDADLG AFESLERLIA EHPADFFAGK SFEPVGACHT
     REAVFASVEL PETPTSPQAH ADHLLHDVFR HVMPVASPTF VGHMTSSLPS FMPSLAKVVA
     ALNQNVVKLE TSGALTGLER QVVGMLHKLV FSQDSAFYGR WLHDADHALG AICSGGTVAN
     LTALWASRNK LLGARDGFAG IHRAGMVAAL RHYGYDGLAI VVSERGHYSL GKAADVLGIG
     RDNLVPVEVD AEGRMRIDLL RDTMRDLQQR NIRPMAIVGI AGTTETGSVD PLDAIADIAQ
     EAGCHFHVDA AWGGATLLSE RERWRFAGIE RADSVVIDAH KQFYVPMGAG MVLFRSPAWT
     QEIIQHANYI VRKGSVDLGR HTLEGSRGAA AVMLYANLHL LGRKGLAQLI DRSIDNAHYF
     ASLIAQQPDF ELVSHPQLCL LTYRYLPETV RAALATASED KREKILDALD ALTVSIQEMQ
     RDAGRSFVSR TQLTSTQFAG RPIAVFRVVL ANPDTTHAIL QDILDEQRML AAASPCMAAL
     MALVEASGRL QR
//