ID   H1S0R7_9BURK            Unreviewed;       481 AA.
AC   H1S0R7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:EHP43926.1};
GN   ORFNames=OR16_06044 {ECO:0000313|EMBL:EHP43926.1};
OS   Cupriavidus basilensis OR16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP43926.1, ECO:0000313|Proteomes:UP000005808};
RN   [1] {ECO:0000313|EMBL:EHP43926.1, ECO:0000313|Proteomes:UP000005808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR16 {ECO:0000313|EMBL:EHP43926.1,
RC   ECO:0000313|Proteomes:UP000005808};
RX   PubMed=22461549; DOI=10.1128/JB.06752-11;
RA   Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA   Nagy I., Horvath B., Nagy I., Kukolya J.;
RT   "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL   J. Bacteriol. 194:2109-2110(2012).
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}.
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:EHP43926.1}.
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DR   EMBL; AHJE01000015; EHP43926.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1S0R7; -.
DR   PATRIC; fig|1127483.3.peg.1208; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000005808; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   481 AA;  51868 MW;  5488CEEE792316F7 CRC64;
     MLDDMLDHLE GIRARPVWQP IPDTVRARFR EPLPREGSGL DQVHETFMDS ILPFAVGNAH
     PGFMGWVHGG GTPVGMLAEM LAAGLNANLG GRDHIPVEVE WQVLRWVIEL FGFPDDASGL
     FLTGSSMANL SGVLVARTRA LGAEVRSTGM AQASRRLTAY TSTRAHGCIA QGMDLAGLGK
     DNLRSIPVDE MGRMDVACLA AAIAVDRAAG FQPFLVVGTA GTVDTGAIDD LAEIARIARR
     ERLHFHVDGA FGALAMLCPQ LAPRLRGIEQ ADSIAFDFHK WLQVPYDAGF FVVRDRQLHL
     RTFATHEGTY LSRGERGMAA GSPWPCDFGP DLSRGFRALK TWFTIKVYGT ERLGGMIAHT
     CRLAQELARR IESEPELELL APVSLNIVCF RFTGAGAEGG SDASRAMEQV NRDLVVALQE
     SGLAAPSSTV LDGRFAIRVA LFNHRSASQD IEALLNATLA LGRSLSATLP VPVPEASALP
     Q
//