ID Q029V0_SOLUE Unreviewed; 470 AA.
AC Q029V0;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:ABJ82176.1};
DE EC=4.1.1.28 {ECO:0000313|EMBL:ABJ82176.1};
GN OrderedLocusNames=Acid_1182 {ECO:0000313|EMBL:ABJ82176.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ82176.1};
RN [1] {ECO:0000313|EMBL:ABJ82176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ82176.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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; CP000473; ABJ82176.1; -; Genomic_DNA.
DR AlphaFoldDB; Q029V0; -.
DR STRING; 234267.Acid_1182; -.
DR KEGG; sus:Acid_1182; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_3_1_0; -.
DR InParanoid; Q029V0; -.
DR OrthoDB; 9803665at2; -.
DR GO; GO:0004058; F:aromatic-L-amino-acid 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 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 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 470 AA; 52036 MW; 930B902DC3712F84 CRC64;
MNPEEFRRRG HQIIDRIADY RANVARYPVM ARTAPGEIKA ALPAEPPENP ESFDEVLADL
DRVVMPGLSH WQHPRFFGYF PSNGELSSVL GDYLSTGLGV LGLSWQSSPA LSEVEEVVTD
WMRQMTGLSA EWSGVIQDTA STCTLVALLC ARERSTGYGL ARGGLQAEAQ PLIVYTSGHS
HSSVDKAALL AGFGRENVRH IASDEKFALR PEALEEAIRE DLAAGRKPCA IAGTTGTTAT
TALDPIADMA RIAREYGLWL HVDAAMAGSA MVLPECRWMW DGIEGADSVV LNPHKWLGAA
FDCSLYYVRG PEHLIRVMST SPSYLRTAAD DQVKNLRDWG LPLGRRFRAL KLWFLIREQG
VKGLQARLRR DLVNAQWLTS AICAEPNWRV LAPVPLQTLC VRHEPPGLEG EALDRHTQAW
ADRINRSGEA YLTPAILEGR WMVRVSVGAL LTEREHVEAL WRLMRKEAGG
//
