ID   TYDC_ORYSJ              Reviewed;         533 AA.
AC   Q94EE9; Q6BD07;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0000303|PubMed:17763868};
DE            Short=OsTyDC {ECO:0000305};
DE            EC=4.1.1.25 {ECO:0000269|PubMed:17763868};
DE   AltName: Full=Trypthophan decarboxylase {ECO:0000303|PubMed:14535886};
GN   Name=TYDC {ECO:0000303|PubMed:17763868};
GN   Synonyms=TDC {ECO:0000303|PubMed:14535886};
GN   OrderedLocusNames=Os01g0770200 {ECO:0000312|EMBL:BAF06290.1},
GN   LOC_Os01g56380 {ECO:0000305};
GN   ORFNames=P0665A11.14 {ECO:0000312|EMBL:BAB56067.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   DOI=10.1007/s10327-004-0151-6;
RA   Ueno M., Kihara J., Honda Y., Isota J., Arase S.;
RT   "DNA fragmentation in Sekiguchi lesion mutants of rice infected with
RT   Magnaporthe grisea.";
RL   J. Gen. Plant Pathol. 70:321-328(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=14535886; DOI=10.1046/j.1365-313x.2003.01875.x;
RA   Ueno M., Shibata H., Kihara J., Honda Y., Arase S.;
RT   "Increased tryptophan decarboxylase and monoamine oxidase activities induce
RT   Sekiguchi lesion formation in rice infected with Magnaporthe grisea.";
RL   Plant J. 36:215-228(2003).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17763868; DOI=10.1007/s00425-007-0614-z;
RA   Kang S., Kang K., Lee K., Back K.;
RT   "Characterization of rice tryptophan decarboxylases and their direct
RT   involvement in serotonin biosynthesis in transgenic rice.";
RL   Planta 227:263-272(2007).
CC   -!- FUNCTION: Catalyzes the decarboxylation of L-tyrosine to tyramine,
CC       which can be converted to the hydroxycinnamic acid amides
CC       feruloyltyramine and 4-coumaroyltyramine (PubMed:17763868). Possesses
CC       low tryptophan decarboxylase activity (PubMed:14535886).
CC       {ECO:0000269|PubMed:14535886, ECO:0000269|PubMed:17763868}.
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:17763868};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P20711};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AB162137; BAD35168.1; -; Genomic_DNA.
DR   EMBL; AP003106; BAB56067.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF06290.1; -; Genomic_DNA.
DR   EMBL; AK065830; BAG89694.1; -; mRNA.
DR   EMBL; AP014957; BAS74545.1; -; Genomic_DNA.
DR   RefSeq; XP_015633932.1; XM_015778446.1.
DR   AlphaFoldDB; Q94EE9; -.
DR   SMR; Q94EE9; -.
DR   STRING; 4530.OS01T0770200-01; -.
DR   PaxDb; Q94EE9; -.
DR   PRIDE; Q94EE9; -.
DR   EnsemblPlants; Os01t0770200-01; Os01t0770200-01; Os01g0770200.
DR   GeneID; 4325604; -.
DR   Gramene; Os01t0770200-01; Os01t0770200-01; Os01g0770200.
DR   KEGG; osa:4325604; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   HOGENOM; CLU_011856_3_1_1; -.
DR   InParanoid; Q94EE9; -.
DR   OMA; CVDLHKW; -.
DR   OrthoDB; 856958at2759; -.
DR   BRENDA; 4.1.1.25; 4460.
DR   PlantReactome; R-OSA-1119344; Hydroxycinnamic acid serotonin amides biosynthesis.
DR   PlantReactome; R-OSA-1119438; Secologanin and strictosidine biosynthesis.
DR   PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004837; F:tyrosine decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:1901695; P:tyramine biosynthetic process; IDA:UniProtKB.
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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..533
FT                   /note="Tyrosine decarboxylase"
FT                   /id="PRO_0000444621"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         281
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         336
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   MOD_RES         339
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   CONFLICT        231
FT                   /note="I -> F (in Ref. 1; BAD35168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="D -> N (in Ref. 1; BAD35168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  57088 MW;  AAD90B5E6B325214 CRC64;
     MAPPSHCHTI NGGAPRNGAI PEVETTTSTP AASDTALLLD ADEFRRLGHQ VVDFIADYYA
     GLGDYPVHPS VTPGFLRRQL PADAPSRPEP EAFAAALRDV RDLILPGVTH WQSPRHFAHF
     PASSSTVGAL GEALAAGINV VPFTWAASPA ATELEMVVVD WLGRALHLPE SLLFAGGGGG
     TILGTSCEAV LCALVAARDR KLAEIGARRI GDLVVYCSDQ THFAFRKAAR IAGIPREHCR
     EIPTCRDDVF ALSPTALHAA MQADVDAGLV PLFLCATVGT TQTTAVDPVR ELCAVAARHG
     GVWVHVDAAY AGSALVCPEF RDVIAGAEAV DSLSMNAHKW LLANNDCCAV WVAAPSALVA
     ALGTEQEYIL RDAAAEGHDV VDYKDWGTTL TRRFRALKVW LVLRCYGVEG LRSHVRSHVA
     MAAAFEAMVR GDARFEVVAP RRFALVCFRL RSPPERLGVG VGVGGEKAAN ELNRRLLEEV
     NAASSGPYMS SAMVGGVYML RCAIGSTLTE ERHVREAWKV VQERATSILR KRG