ID   A0A0P7AHU8_9FLAO        Unreviewed;       476 AA.
AC   A0A0P7AHU8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:KPM33157.1};
GN   ORFNames=I595_58 {ECO:0000313|EMBL:KPM33157.1};
OS   Croceitalea dokdonensis DOKDO 023.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceitalea.
OX   NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM33157.1, ECO:0000313|Proteomes:UP000050280};
RN   [1] {ECO:0000313|EMBL:KPM33157.1, ECO:0000313|Proteomes:UP000050280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM33157.1,
RC   ECO:0000313|Proteomes:UP000050280};
RA   Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT   "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT   023 that contains proton- and sodium-pumping rhodopsins.";
RL   Submitted (SEP-2015) 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}.
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:KPM33157.1}.
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DR   EMBL; LDJX01000001; KPM33157.1; -; Genomic_DNA.
DR   RefSeq; WP_054557388.1; NZ_LDJX01000001.1.
DR   AlphaFoldDB; A0A0P7AHU8; -.
DR   STRING; 1300341.I595_58; -.
DR   PATRIC; fig|1300341.3.peg.60; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000050280; Unassembled WGS sequence.
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; 3.90.1150.170; -; 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   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:UP000050280}.
FT   MOD_RES         298
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   476 AA;  54039 MW;  0C33E87BF8AA9D11 CRC64;
     MKNQLLEKAF DVRLFEKHLL QIIPILKKHL FNTTKGKNDF TLNYTQPLDQ LNFWEDYLEH
     GVPEEMLDEV FKRTTHTHHP KYVGHQVSAP APITILTAMV SSLLNNGMAV YEMGMAPTAI
     EKVVVDILCK KIGYSDNFGG FLTSGGTLAN LTALLSARKA MVKHDVWNHG HQDSLGVMVC
     EQAHYCIDRA AKIMGLGQKG IIKIPARNTF AMDIAQLEYG YQEAVQKGIH IFAIVGSAPS
     TATGAYDDLE AIANFARNKN IWFHVDGAHG GAAIFSDKYR FLLNGIAKAD SVVIDGHKMM
     LMPTITTALL FKDKKRAQQT FSQKADYLLD DMEDDWINSG KRTFECTKTM MGMHWFILLK
     FYGEKLFDDF VTRQYDLARA FQKLLENHPQ FELATPLMAN IVCFRWVNGN FDQEELNRLN
     QTIRQHLLED GEYYLVQTKL GDTNYLRTSL MNPFTELSHL EHLLGKIDAM AVKLTN
//