ID   T1KIS9_TETUR            Unreviewed;       844 AA.
AC   T1KIS9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur12g02440.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur12g02440.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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DR   EMBL; CAEY01000114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1KIS9; -.
DR   STRING; 32264.T1KIS9; -.
DR   EnsemblMetazoa; tetur12g02440.1; tetur12g02440.1; tetur12g02440.
DR   eggNOG; KOG0628; Eukaryota.
DR   HOGENOM; CLU_807345_0_0_1; -.
DR   Proteomes; UP000015104; 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   CDD; cd06450; DOPA_deC_like; 1.
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; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999:SF177; MIP05841P; 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};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104}.
FT   REGION          19..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         541
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   844 AA;  95293 MW;  A41E4C7A5350B226 CRC64;
     MCYSRLFGDC HLFFRKANSS DQSPDLDETV PLKESSVGDN VNESCNNHKL AFKSTEYEKL
     MESPTKSRRD SSNNIHQPTT FASISSLVRD IFRNDLKYPA ATTQSTKSNT PSPTLDIKLS
     SSSNPTKATT NNSNNSLTNH HPTCNCSTFN GNNNNVNRLK SNGDSLNNFN SKRINRIKIK
     DEKKLDTDDD DNNDTNYDHN QGVKSSHNHY DDHSIQANFT KCFYPDKKST SEAPFCGMDS
     KEWRVRGKEM VDYIANYLET IDQRRVTPNV EPGYLKPQLP EEAPLKAEQW DTIMEDFNKL
     IMPGITHWQH PRFHAYFPAG NAYPSILADM LSDAISCIGF SWAASPSCTE LETIMLDWMG
     RAIGLPDKFM CFAENSKGGG VIEGSASECI LVTLLAARYE AVKQAKKQEP NAKDTDILGK
     LIAYCSKEAH SSVEKAAMIG FVKLRILDTD EKFRMRPDLL EKSIQEDKAQ GFIPFWAAIT
     LGSTSCCSVD PVDSVGMICQ KEGVWLHVDA AYGGSSLICP EFQYLLKGIE LASSFNMNPN
     KWMLINFDCS LLWVTDRFKL TQALVVDPLY LQHSYSDKAI DYRHWGIPLS RRFRSLKLWF
     VIRNYGIEGL QKYIRNHCRL AKKFENLMRQ DERFEIMNEV IFGLVCFRLK GSDTLNKKLL
     SSINASGEMH MVPANLGNKY VIRFCVCSQH ATEDDISAAY EIISQFSANL LAIIGSEESM
     AALQQQQAVI QGDLTGSQQQ QFTKQESQKS SIEEKEGSIE IKGGLSIDKI ETTPEEETKK
     ETEDEMPDEV IVFDRKINTS LKYRRSFFVR MVSDPKLYNP KIVKALSCSS DQTDDKDTGI
     LSPI
//