ID   E6PI80_9ZZZZ            Unreviewed;       476 AA.
AC   E6PI80;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Aromatic amino acid decarboxylase {ECO:0000313|EMBL:CBH76170.1};
GN   Name=ddc {ECO:0000313|EMBL:CBH76170.1};
GN   ORFNames=CARN1_0650 {ECO:0000313|EMBL:CBH76170.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH76170.1};
RN   [1] {ECO:0000313|EMBL:CBH76170.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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:CBH76170.1}.
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DR   EMBL; CABL01000019; CBH76170.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6PI80; -.
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}.
SQ   SEQUENCE   476 AA;  53054 MW;  5CF80A0708C1583E CRC64;
     MDGQQRIEED FARVGRWVAR YFHHPEEFRV FPDVRPGEVL ARLPDRAPED PEGFEEILRD
     FERIVVPATT HWNHPRFFAY FATSADPAAV MAEALAATLD VKAMLWRTSP AATELETAMM
     IWLRRLLGLP EQFTGAIYDT ASIAGFTALA AARESLGLDI RRRGATGRDL PTLRIYATEH
     THSHVAKAAI ALGIGHANVV EVPCDERFRM RPEALESAIR HDVRSGMRPM AIVATVGTTS
     TTSVDPIPGI AAIAETHKIW LHVDAAYAGA AGMLPECEWL LEGCEQADSL VLNPHKWLFV
     PMDCSVLFVR DIEQLRRSFS LVPEYLRAGD DGVTNYMDYG LQLGRRFRAL KLWFVFRALG
     ARRIRETLRG HISMAAAFAA WVTEEPNWEV MAPHPLSVIC FRHVPSGMEP EQLDAHNADL
     LAAANATGEM FISHTVLKGS YALRLAIGNQ RSTLEDVEAA WAILRRCATS LEAVPR
//