ID   A0A0C5WU90_9GAMM        Unreviewed;       533 AA.
AC   A0A0C5WU90;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Putative pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:AJR06625.1};
GN   ORFNames=H744_1c1607 {ECO:0000313|EMBL:AJR06625.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06625.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR06625.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR06625.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) 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; CP005973; AJR06625.1; -; Genomic_DNA.
DR   RefSeq; WP_052829672.1; NZ_CP005973.1.
DR   AlphaFoldDB; A0A0C5WU90; -.
DR   STRING; 658445.H744_1c1607; -.
DR   KEGG; pgb:H744_1c1607; -.
DR   PATRIC; fig|658445.3.peg.1737; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000032303; Chromosome 1.
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; 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   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:UP000032303}.
FT   MOD_RES         341
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   533 AA;  58819 MW;  5C29E5E0EE3D3788 CRC64;
     MSLLECRLER ELLSTEEESA IAQVGKAREL YQLSFSGRLG HDLPRHGNKE KINSGLKLST
     SRHRFDRVDI GNQPVAPFEY LDFLETVVFP HTVNTFSTKF LGHMTAPLPE FITEVAGVIS
     RMNQNQVKVE TSNVLTLLER QVLGAVHHKI YRKQAGFYES YMQCPESCLG VVTGGGTLAN
     ITSLSYALNS AFRADGNFAG LTKEGLVSAL NHYGFKDVVV IGSKRMHYSV DKAAKLLGLG
     ERNVIRLETD SHGRVDLAQM RSNLEECRKG KIHVLALIGI AGATETGSVD PLEEIGALAA
     EFGVHFHADA AWGGAYTLSS NHRELVKGIE MADTVTICAH KQLYIPMGTS LCIFKSPGFA
     SHSENNTAYQ CKKGSYDLGR YTIEGSRPAS ILMLHALLNL WGDAGMGHVF DTTLSLTQNF
     TGKIKSSENF LLVQEPALNI VVYRYIPVTL REKVLTKEKL TYAEIELINE INKKIQSEQF
     INGNSFVSST TLVNGEEEVV VFRAVFCNPL TRENDLDALL ADQAKIARDI EIA
//