ID   B6EHQ6_ALISL            Unreviewed;       547 AA.
AC   B6EHQ6;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:CAQ79717.1};
DE            EC=4.1.1.- {ECO:0000313|EMBL:CAQ79717.1};
GN   OrderedLocusNames=VSAL_I2032 {ECO:0000313|EMBL:CAQ79717.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ79717.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ79717.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ79717.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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; FM178379; CAQ79717.1; -; Genomic_DNA.
DR   RefSeq; WP_012550578.1; NC_011312.1.
DR   AlphaFoldDB; B6EHQ6; -.
DR   KEGG; vsa:VSAL_I2032; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000001730; 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}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   547 AA;  61325 MW;  20C3C30F218E245F CRC64;
     MVTDNKTADA NLESMLRIFT VPEAPDSTLG KIEQELSQNL NQFLREHIVA EEKPLTEIEK
     DFTDSSMPEY PTYVSEHTEH LLETVVSQSV HTSAPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHRLIYGQ ESAFYERWMH SADHSLGAFC SGGTIANITA
     LWVARNRLLQ PEGNFKGIAQ EGLFAALTHY KYSGLAIFVS ERGHYSVKKA ADVLGIGQDS
     VIPVKTDNNN RICLHDLKLK MAQAKEKNIK PLAIIGVAGT TETGTIDPLR ALAEVAKQVN
     CHFHVDAAWG GATLMSNQYR YLLDGIDLAD SVTIDAHKQL YVPMGAGMVI FKDPELMSSI
     QHHAEYILRK GSKDLGRHTL EGSRSGMAML LYSCFNVISR PGYELLINQS IEKAKYFAEI
     IDQQDDFEVI TQPELCLLTY RYIPKNVTLA LTKANPEQTI EIYDHLDELT KFIQKTQRET
     GKSFVSRTRL TPEAYQNMPT IVFRVVLANP LTTKEILHSV LIEQREIAQK SEISLPQLTK
     LADSILK
//