ID   A0A0P1G3P0_9RHOB        Unreviewed;       465 AA.
AC   A0A0P1G3P0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:CUH76335.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:CUH76335.1};
GN   Name=ddc {ECO:0000313|EMBL:CUH76335.1};
GN   ORFNames=TRN7648_00883 {ECO:0000313|EMBL:CUH76335.1};
OS   Tropicibacter naphthalenivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tropicibacter.
OX   NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH76335.1, ECO:0000313|Proteomes:UP000054935};
RN   [1] {ECO:0000313|EMBL:CUH76335.1, ECO:0000313|Proteomes:UP000054935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH76335.1,
RC   ECO:0000313|Proteomes:UP000054935};
RG   Swine Surveillance;
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CYSE01000002; CUH76335.1; -; Genomic_DNA.
DR   RefSeq; WP_058246440.1; NZ_FWXX01000002.1.
DR   AlphaFoldDB; A0A0P1G3P0; -.
DR   STRING; 441103.TRN7648_00883; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000054935; 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:UP000054935}.
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   465 AA;  50860 MW;  0BFE10192A1097A3 CRC64;
     MDWDEFSKWG KQIADWGADY HKTLRDRPVR AQTKPGEIAA QLPEAPPEAP EAMDAIMADF
     ERVVMPGLTH WQHPRFFAYF PANAAPPSML AEMLVTVLAP QCMLWQTSPA ATEMEQRMLD
     WLRQAIGLPA DFSGVIQDSA SSATLAAVLV MRERALDWQG NTRGLAGGAA PRVYCSGQVH
     TSIDRAIWVS GIGQENLVKI ASLDAPRRPL DVDALRAQIM ADRAAGHIPA GIIGATGGTS
     IGGCDDIAAL AEVAAEEGLY LHVDAAWAGA AMICPEYRDL WAGVERADSV VFNPHKWLGA
     QFDCSAHFIR DPDALRQTLA IRPEYLKTHA QQEVTDFSEW SVPLGRRFRA LKLWFLIRAY
     GLDGLRAMIR NHVAWSGQVC EGLRAAGFEI VSEPVLSLFS FRTSGDDARN LALVEAINAD
     GRIYLTQTLV DGRTAIRFQA GAFGMTEADA AIALDVIQEI NRSLP
//