ID   A0A0D6MTC3_ACEAC        Unreviewed;       492 AA.
AC   A0A0D6MTC3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:GAN56939.1};
GN   ORFNames=Abac_012_013 {ECO:0000313|EMBL:GAN56939.1};
OS   Acetobacter aceti NBRC 14818.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX   NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN56939.1, ECO:0000313|Proteomes:UP000032677};
RN   [1] {ECO:0000313|EMBL:GAN56939.1, ECO:0000313|Proteomes:UP000032677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN56939.1,
RC   ECO:0000313|Proteomes:UP000032677};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acetobacter aceti NBRC 14818.";
RL   Submitted (NOV-2012) 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:GAN56939.1}.
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DR   EMBL; BAMU01000012; GAN56939.1; -; Genomic_DNA.
DR   RefSeq; WP_010666586.1; NZ_SLZP01000012.1.
DR   AlphaFoldDB; A0A0D6MTC3; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000032677; 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; 3.90.1150.170; -; 2.
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   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}.
FT   MOD_RES         307
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   492 AA;  53132 MW;  291440FD806A01DD CRC64;
     MVDDTDPFLS LDPQGADWDR LRATGHHMLD MMFDNLREIR EQPVWQPLPD DIRTGFRHTP
     VPEHGMDAEA FGETFKQMVL PYSVGNRHPG FMGWVHGGGT PVGMLAEMLA AGLNANLGGR
     DHAPVEVERM VIRWASSLMG FPETASGLFV TGSSMANFIA VIVASRAAKD GLSLRQNGVG
     QRSLVGYAAC SAHGCISRAF DLAGLGSDAL RLVPVDDAFR MDTTALKAMI AADRQAGFEP
     FLVVGTAGTV DVGAIDPLDV ISGIATKEEL WFHVDGAFGA MAALSPHFKK ALSGLERADS
     LAFDFHKWAQ VPYDAGCVIV RDATKHAAAF AQTLSYLSRE DRGLAAGAPW FCDLGPDLSR
     GFRALKVWAT LSVYGTQRLG RMVDHCCAVA RHLEARVDAE PMLELMAPVT LDIVCFRLRD
     CTLTDEQLDH LNGEIVKDVQ IAGLAVPSTT RINGRLVIRA AIVNHRTMAA DVDRMVDAVL
     AFAARRGLTA PG
//