ID   Q6LS17_PHOPR            Unreviewed;       549 AA.
AC   Q6LS17;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Hypothetical Glutamate decarboxylase {ECO:0000313|EMBL:CAG19909.1};
GN   Name=SO1769 {ECO:0000313|EMBL:CAG19909.1};
GN   OrderedLocusNames=PBPRA1498 {ECO:0000313|EMBL:CAG19909.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG19909.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378667; CAG19909.1; -; Genomic_DNA.
DR   RefSeq; WP_011218230.1; NC_006370.1.
DR   AlphaFoldDB; Q6LS17; -.
DR   STRING; 298386.PBPRA1498; -.
DR   KEGG; ppr:PBPRA1498; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000000593; 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; 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:UP000000593}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   549 AA;  61308 MW;  A2B793E026ADF5A6 CRC64;
     MAVDNRKADA TLESLHRIFT VPEAPESTLG LIEQKISQNL NEFLGTHIAA REKPLIEIEK
     DFSSAEIPEN PSFVSDHTQF LLTKLVAQSV HTSAPSFIGH MTSALPYFLM PLSKIMIGLN
     QNLVKIETSK AFTPLERQVL GMMHNLIFNE ETSFYQQWMH SADHSLGAFC SGGTIANITA
     LWVARNNVLK PDGEFKGVAN EGLFRAMKHY GYDDLAILVS ERGHYSLKKA ADVLGIGRDC
     LIPIKTDDNN RIRVDDLTAT LQSLKEKNIK PFAIIGVAGT TETGNIDPLD ELADIAQAHD
     CHFHVDAAWG GATLMSNKYR SLLKGIERAD SITIDAHKQL YVPMGAGMVI FKNPALMTSI
     EHHAEYILRK GSKDLGSHTL EGSRSGMAML LFASLNIISR QGYEMLINNS IDKAKHFANM
     VKQDPDFELV TEPELCLLTY RYVPAETQQA LTIANAEDKH LLHDALNDLT KFIQKRQRES
     GKSFVSRTRL TPEKWDHKIT TVFRVVLANP LTTDNILQDV LIEQKELAKE SVHSLPRLFT
     LTKRILANN
//