ID R7SB87_TREMS Unreviewed; 534 AA.
AC R7SB87;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TREMEDRAFT_70540 {ECO:0000313|EMBL:EIW65462.1};
OS Tremella mesenterica (strain ATCC 24925 / CBS 8224 / DSM 1558 / NBRC 9311 /
OS NRRL Y-6157 / RJB 2259-6 / UBC 559-6) (Jelly fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Tremellaceae; Tremella.
OX NCBI_TaxID=578456 {ECO:0000313|EMBL:EIW65462.1, ECO:0000313|Proteomes:UP000054539};
RN [1] {ECO:0000313|Proteomes:UP000054539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fries {ECO:0000313|Proteomes:UP000054539};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH711552; EIW65462.1; -; Genomic_DNA.
DR RefSeq; XP_007008636.1; XM_007008574.1.
DR AlphaFoldDB; R7SB87; -.
DR GeneID; 18498329; -.
DR KEGG; tms:TREMEDRAFT_70540; -.
DR VEuPathDB; FungiDB:TREMEDRAFT_70540; -.
DR eggNOG; KOG0628; Eukaryota.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000054539; 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 PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
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:UP000054539}.
FT MOD_RES 344
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 534 AA; 59194 MW; C667F485C4B249D9 CRC64;
MTLASLVGLD RSCPCYAAVD AICDYYTHLD RRPVKAEVEP GYLLAQLPGE APQTGQPFPS
IARDFQRLIL PGITHWQHPS FFAYFPAIST FESMLGDLYA ASVSNPGFNW VCSPACTELE
QVVMDWMAKI LGLHPSFHIG SGKGGGIISV RWSNISPVGD VTRLKSREPL QKQLSQLQWR
PGKGLYGISA TVLTSPGMDA VPGSPISNEV REKWSQKLVM YGSTQTHSIA AKAARLLGLR
FRAVHVTAAD GYALRGDALR EAIEADVATD LVPFFVVATI GTTSTGAVDH IADIGQVLNS
YPTAFLHVDA AWAGMAYALP EYRAKLRLDE VNTYAHSFCA NAHKWGLVGF DYSLFYIRDR
KDLTEALDVT PAFLRSKEGD SGIVIDYRNW QLALGRRFRN VKLWFVLRSY GVDGLQKHLR
SGIHHCRKLA DRIRSSKDFK LVAEPSLSLL VFRLQPQGYE GGEDDDLNRL NKTLHERLMA
RSDVFLTRTV IKTEEGEMTC IRFAMGGLKT TLECVNATWD VVEQEGAAVF AKDE
//
