ID A0A087SQR1_AUXPR Unreviewed; 493 AA.
AC A0A087SQR1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Tyrosine decarboxylase 1 {ECO:0000313|EMBL:KFM28065.1};
GN ORFNames=F751_5176 {ECO:0000313|EMBL:KFM28065.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM28065.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM28065.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM28065.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
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; KL662162; KFM28065.1; -; Genomic_DNA.
DR RefSeq; XP_011401077.1; XM_011402775.1.
DR AlphaFoldDB; A0A087SQR1; -.
DR STRING; 3075.A0A087SQR1; -.
DR GeneID; 23616567; -.
DR KEGG; apro:F751_5176; -.
DR eggNOG; KOG0628; Eukaryota.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000028924; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 493 AA; 53667 MW; C41E0400B99E7263 CRC64;
MSDTPGTSAG TGAEDYEHPI SHEDFRQLGY KMIDAIVDYR SNIEKHPVRS EVAPGYLAEK
LPESAPTQPE GLDAILSDVQ THIMPGITHW QHPSFFSWYP ANSSYPALLG DMLSSALGVV
GFAWIGSPAA TELETVTLDW LARFLRLPNA FLSTGTTGGG GVIQGTASEA ALVALLAARA
RPLDGRDPGA DGPRLVAYTT DQAHSCVKKA CAVAGIQHLR LLPTSAERGW ALDPATLEAA
MTADEGHGLM PFFLTTLIGT TSSAAVDPVA ELAAVARRHG AWVHVDAAYA GVFACLPDQH
DLYFQGLEGV DSFSTNPHKG MLVTFDCSAL WVQNSFWLRT ALSLEPQFQF AGLRHAAEHL
DYKDWQVPLG RRFRALKLWF VLRMYGTERL QAYLRHHLDM AKALAQLVEA DPAFDIIATP
RFGLVCFAPR GASEEESTAL LERVNASGRT FMVHTRLGGR HVWRLAVGGV HTQWRHVEEV
WALVQKVVGG GEA
//
