ID   A0A1Y6KU53_9GAMM        Unreviewed;       554 AA.
AC   A0A1Y6KU53;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:SMY15713.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:SMY15713.1};
GN   Name=ddc_1 {ECO:0000313|EMBL:SMY15713.1};
GN   ORFNames=PAQU9191_00936 {ECO:0000313|EMBL:SMY15713.1};
OS   Photobacterium aquimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY15713.1, ECO:0000313|Proteomes:UP000196485};
RN   [1] {ECO:0000313|Proteomes:UP000196485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA   Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL   Submitted (JUN-2017) 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; FYAH01000001; SMY15713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6KU53; -.
DR   Proteomes; UP000196485; Unassembled WGS sequence.
DR   GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
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:UP000196485}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   554 AA;  61926 MW;  9A059EADB377AC38 CRC64;
     MATNNRTADA SLESLHRIFT VPEAPDSTLG LIEKELSENL NEFLRTHIAA TEKPLAEIEK
     DFSNANIPEV PSFVSDHTQL LLNKLVAQSV HTAAPTFIGH MTSALPYFMM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHKLIFNQ NESFYQQWMH SADHSLGAFC SGGTIANITA
     LWVARNAALQ PDGEFTGVGQ QGLLRAMRHY GYDDLAILVS ERGHYSLKKA ADVLGIGRDS
     LIAIKTDDNN RVDLDALQTT LTDLKRNNIK PFAIIGIAGT TETGNIDPLD QLADIAAEHQ
     CHFHVDAAWG GATLMSNKYR HLLKGIERAD SITIDAHKQL YIPMGAGMVI FKNPELMTAI
     EHHAEYILRK GSKDLGSHTL EGSRSGMAML LYASMNIISR PGYELLINNS IEKAHYFAHC
     IEQHPDFELV THPELCLLTY RYVPAKTQQA LLHATPEQRD QLLELLNDLT QFIQKRQRES
     GKSFVSRTRI TPEKWQRKPT TVFRVVLANP LTTTEILENV LIEQQQLAQQ STISLPEIIT
     LTDQITKKST KIDI
//