ID   A0A1N7KFQ3_9RHOB        Unreviewed;       465 AA.
AC   A0A1N7KFQ3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:SIS60412.1};
GN   ORFNames=SAMN05421759_101714 {ECO:0000313|EMBL:SIS60412.1};
OS   Roseivivax lentus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=633194 {ECO:0000313|EMBL:SIS60412.1, ECO:0000313|Proteomes:UP000186684};
RN   [1] {ECO:0000313|EMBL:SIS60412.1, ECO:0000313|Proteomes:UP000186684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29430 {ECO:0000313|EMBL:SIS60412.1,
RC   ECO:0000313|Proteomes:UP000186684};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-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; FTOQ01000001; SIS60412.1; -; Genomic_DNA.
DR   RefSeq; WP_076445014.1; NZ_FTOQ01000001.1.
DR   AlphaFoldDB; A0A1N7KFQ3; -.
DR   STRING; 633194.SAMN05421759_101714; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000186684; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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   InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   465 AA;  52161 MW;  5BECDF76EA0A3C2E CRC64;
     MDWDEFEEWG RYVSRWAADY HKSLRDLPVR AQTRPGDTIR GLAAAPPSQG QPMDAIIDDF
     ERVVMPGMTH WQHPRFFAYF PANATPPSMI AEMLVTTIAA QCMLWQTSPA ATEMETVMVD
     WLRQALALPE EYTGVIQDSA SSATLSAVLT MRERAIDYTG NRDGLNGKGT LRIYCSEQVH
     SSIDRAAWIA GIGQENLVKL PTRSPRHELD VDALRAAIRG DRAAGHIPAG IITITGGTGV
     GASDDLAAVL DVARTEDLYT HLDAAWAGAA MICEEFREEF WAGVAGYDSI VINPHKWLGA
     QFDCSVQFLR DPQPQLNTLK IEPEYLKTTG AAVTNYSEWT IPLGRRFRAL KLWFLIRSYG
     LEGLKARLRN HVRWANEICD VLRAMDGFDI VTEPMLSLFT FRCPGDDKDQ QRLVDAINDD
     GRIYLTQGAF QGKKVIRFQV GQFETTREDV LFAADVIRDV WARMK
//