ID   A0A238LC17_9RHOB        Unreviewed;       489 AA.
AC   A0A238LC17;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:SMY06955.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:SMY06955.1};
GN   Name=ddc_1 {ECO:0000313|EMBL:SMY06955.1};
GN   ORFNames=LOM8899_01085 {ECO:0000313|EMBL:SMY06955.1};
OS   Flavimaricola marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Flavimaricola.
OX   NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY06955.1, ECO:0000313|Proteomes:UP000201613};
RN   [1] {ECO:0000313|EMBL:SMY06955.1, ECO:0000313|Proteomes:UP000201613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8899 {ECO:0000313|EMBL:SMY06955.1,
RC   ECO:0000313|Proteomes:UP000201613};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; FXZK01000001; SMY06955.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238LC17; -.
DR   Proteomes; UP000201613; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
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; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
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:UP000201613}.
FT   MOD_RES         307
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   489 AA;  52787 MW;  5B90859BC1B8C33D CRC64;
     MARIREDASE ISLDPDNWDE MRRLAHGMVD DAIARLQGLR DGPVWQPMPA ATRQGFEGPP
     PAKGTPLDAV YADVTGTLYP YAMGNIHPRF WGWYMGAGCL TGALADFLAG VDGTNLGGGD
     TGAAQVDLQV TDWLRQMMGF PEGASGILVN AGSMANIVGL TAARNAMAGV DLHQQSVADI
     AAPLRFYASD QVHNCHMKAM NLLGLGAKAL VRVPTDDAFQ MDMDALRKAI QADREAGLRP
     ACVIATAGTT NTSSIDPVPE IADLCGEEGL WLHVDGCIGA MFAIAPESRH LVAGIDRADS
     LALDLHKGLQ APFDVGCALV RDRRIHRATF AEDAEYLQVA TRGLAAAEFL HDYGPETSRG
     FRALKVWMML RQFGVETFGR MLDQTVAQAR HLTSLVEKEP QLALMAPTVA AVVCFRHEPD
     GLDEAGLRAH NTEIMLRLQE TGIAVISDTT LRGRHCLRVA ICNHRTRSED LDLLVAEVLR
     IGADLLQPA
//