TYDC_PAPSO
ID TYDC_PAPSO Reviewed; 512 AA.
AC O82415; A0A3S7SKR6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Tyrosine decarboxylase {ECO:0000303|PubMed:23204519};
DE Short=PsTyDC {ECO:0000303|PubMed:23204519};
DE EC=4.1.1.25 {ECO:0000269|PubMed:23204519};
GN Name=TYDC {ECO:0000303|PubMed:23204519};
GN Synonyms=TYDC9 {ECO:0000312|EMBL:AAC61842.1};
GN ORFNames=C5167_008148 {ECO:0000312|EMBL:RZC64467.1};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Marianne;
RX PubMed=9733527; DOI=10.1104/pp.118.1.69;
RA Facchini P.J., Penzes-Yost C., Samanani N., Kowalchuk B.;
RT "Expression patterns conferred by tyrosine/dihydroxyphenylalanine
RT decarboxylase promoters from opium poppy are conserved in transgenic
RT tobacco.";
RL Plant Physiol. 118:69-81(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN
RP COMPLEX WITH L-TYROSINE AND PYRIDOXAL PHOSPHATE, SUBUNIT, AND MUTAGENESIS
RP OF HIS-205 AND TYR-350.
RA Torrens-Spence M.P., Chiang Y.-C., Smith T., Vicent M.A., Wang Y.,
RA Weng J.K.;
RT "Structural basis for independent origins of new catalytic machineries in
RT plant AAAD proteins.";
RL Submitted (AUG-2018) to the PDB data bank.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HN1;
RX PubMed=30166436; DOI=10.1126/science.aat4096;
RA Guo L., Winzer T., Yang X., Li Y., Ning Z., He Z., Teodor R., Lu Y.,
RA Bowser T.A., Graham I.A., Ye K.;
RT "The opium poppy genome and morphinan production.";
RL Science 362:343-347(2018).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF TYR-350.
RX PubMed=23204519; DOI=10.1074/jbc.m112.401752;
RA Torrens-Spence M.P., Liu P., Ding H., Harich K., Gillaspy G., Li J.;
RT "Biochemical evaluation of the decarboxylation and decarboxylation-
RT deamination activities of plant aromatic amino acid decarboxylases.";
RL J. Biol. Chem. 288:2376-2387(2013).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-101; CYS-170; ASN-318; ALA-319 AND
RP SER-372.
RX PubMed=25107664; DOI=10.1016/j.phytochem.2014.07.007;
RA Torrens-Spence M.P., Lazear M., von Guggenberg R., Ding H., Li J.;
RT "Investigation of a substrate-specifying residue within Papaver somniferum
RT and Catharanthus roseus aromatic amino acid decarboxylases.";
RL Phytochemistry 106:37-43(2014).
CC -!- FUNCTION: Converts tyrosine into tyramine, a precursor of isoquinoline
CC alkaloids and various amides. {ECO:0000269|PubMed:23204519,
CC ECO:0000269|PubMed:25107664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:327995; EC=4.1.1.25;
CC Evidence={ECO:0000269|PubMed:23204519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346;
CC Evidence={ECO:0000269|PubMed:23204519};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:23204519};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AF025433; AAC61842.1; -; Genomic_DNA.
DR EMBL; MG748690; AYA72253.1; -; mRNA.
DR EMBL; CM010720; RZC64467.1; -; Genomic_DNA.
DR PDB; 6EEM; X-ray; 2.61 A; A/B=1-512.
DR PDBsum; 6EEM; -.
DR AlphaFoldDB; O82415; -.
DR SMR; O82415; -.
DR EnsemblPlants; RZC64467; RZC64467; C5167_008148.
DR Gramene; RZC64467; RZC64467; C5167_008148.
DR OMA; YKTPSRK; -.
DR BRENDA; 4.1.1.28; 4515.
DR Proteomes; UP000316621; Chromosome 6.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..512
FT /note="Tyrosine decarboxylase"
FT /id="PRO_0000450477"
FT BINDING 100
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6EEM"
FT BINDING 205
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6EEM"
FT BINDING 320
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6EEM"
FT BINDING 350
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6EEM"
FT MOD_RES 321
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 101
FT /note="S->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:25107664"
FT MUTAGEN 170
FT /note="C->S: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:25107664"
FT MUTAGEN 205
FT /note="H->N: Acquires the capacity to produce 4-
FT hydroxyphenylacetaldehyde from L-tyrosine."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 318
FT /note="N->S: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:25107664"
FT MUTAGEN 319
FT /note="A->P: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:25107664"
FT MUTAGEN 350
FT /note="Y->F: Acquires the capacity to produce 4-
FT hydroxyphenylacetaldehyde from L-tyrosine."
FT /evidence="ECO:0000269|PubMed:23204519, ECO:0000269|Ref.2"
FT MUTAGEN 372
FT /note="S->G: Acquires the capacity to produce 5-
FT hydroxytryptamine from 5-hydroxytryptophan."
FT CONFLICT 45
FT /note="K -> N (in Ref. 1; AAC61842)"
FT CONFLICT 202
FT /note="D -> N (in Ref. 1; AAC61842)"
FT CONFLICT 348
FT /note="P -> A (in Ref. 1; AAC61842)"
FT CONFLICT 410
FT /note="I -> M (in Ref. 1; AAC61842)"
FT CONFLICT 434
FT /note="T -> A (in Ref. 1; AAC61842)"
FT CONFLICT 456
FT /note="V -> A (in Ref. 1; AAC61842)"
FT HELIX 22..42
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 128..145
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:6EEM"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:6EEM"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:6EEM"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 389..411
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 445..465
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:6EEM"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:6EEM"
FT HELIX 492..509
FT /evidence="ECO:0007829|PDB:6EEM"
SQ SEQUENCE 512 AA; 56555 MW; F7D05CBE46734DDB CRC64;
MGSLPTNNLE SISLCSQNPL DPDEFRRQGH MIIDFLADYY KNVEKYPVRS QVEPGYLKKR
LPESAPYNPE SIETILEDVT NDIIPGLTHW QSPNYFAYFP SSGSIAGFLG EMLSTGFNVV
GFNWMSSPAA TELESIVMNW LGQMLTLPKS FLFSSDGSSG GGGVLQGTTC EAILCTLTAA
RDKMLNKIGR ENINKLVVYA SDQTHCALQK AAQIAGINPK NVRAIKTSKA TNFGLSPNSL
QSAILADIES GLVPLFLCAT VGTTSSTAVD PIGPLCAVAK LYGIWVHIDA AYAGSACICP
EFRHFIDGVE DADSFSLNAH KWFFTTLDCC CLWVKDSDSL VKALSTSPEY LKNKATESKQ
VIDYKDWQIA LSRRFRSMKL WLVLRSYGVA NLRTFLRSHV KMAKHFQGLI GMDNRFEIVV
PRTFAMVCFR LKPTAIFKQK IVDNDYIEDQ TNEVNVKLLE SVNASGKIYM THAVVGGVYM
IRFAVGATLT EERHVTGAWK VVQEHTDAIL GA
