TDC2_ORYSJ
ID TDC2_ORYSJ Reviewed; 497 AA.
AC Q7XHL3; Q0D6V0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Tryptophan decarboxylase 2 {ECO:0000303|PubMed:17763868};
DE EC=4.1.1.- {ECO:0000269|PubMed:17763868};
GN Name=TDC2 {ECO:0000303|PubMed:17763868};
GN OrderedLocusNames=Os07g0437500 {ECO:0000312|EMBL:BAT01249.1},
GN LOC_Os07g25590 {ECO:0000305};
GN ORFNames=OSJNBa0026I22.3 {ECO:0000312|EMBL:BAD30830.1},
GN OSJNBb0095H08.30 {ECO:0000312|EMBL:BAC80122.1};
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 [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 [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP FUNCTION.
RX PubMed=19439571; DOI=10.1104/pp.109.138552;
RA Kang K., Kim Y.S., Park S., Back K.;
RT "Senescence-induced serotonin biosynthesis and its role in delaying
RT senescence in rice leaves.";
RL Plant Physiol. 150:1380-1393(2009).
CC -!- FUNCTION: Involved in serotonin biosynthesis. Catalyzes the
CC decarboxylation of L-tryptophan to tryptamine, which is converted to
CC serotonin by tryptamine 5-hydroxylase (PubMed:17763868). May play a
CC minor role in serotonin biosynthetis during senescence. Accumulation of
CC serotonin attenuates leaf senescence (PubMed:19439571).
CC {ECO:0000269|PubMed:17763868, ECO:0000269|PubMed:19439571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-tryptophan = CO2 + tryptamine; Xref=Rhea:RHEA:30339,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57887,
CC ChEBI:CHEBI:57912; 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; AP005101; BAD30830.1; -; Genomic_DNA.
DR EMBL; AP005783; BAC80122.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21423.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01249.1; -; Genomic_DNA.
DR EMBL; AK103253; BAG95977.1; -; mRNA.
DR RefSeq; XP_015644906.1; XM_015789420.1.
DR AlphaFoldDB; Q7XHL3; -.
DR SMR; Q7XHL3; -.
DR STRING; 4530.OS07T0437500-01; -.
DR PaxDb; Q7XHL3; -.
DR PRIDE; Q7XHL3; -.
DR EnsemblPlants; Os07t0437500-01; Os07t0437500-01; Os07g0437500.
DR GeneID; 4343080; -.
DR Gramene; Os07t0437500-01; Os07t0437500-01; Os07g0437500.
DR KEGG; osa:4343080; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; Q7XHL3; -.
DR OMA; NPGFNWS; -.
DR OrthoDB; 856958at2759; -.
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 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q7XHL3; baseline and differential.
DR Genevisible; Q7XHL3; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0036469; F:L-tryptophan decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; 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 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 Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome;
KW Serotonin biosynthesis.
FT CHAIN 1..497
FT /note="Tryptophan decarboxylase 2"
FT /id="PRO_0000247498"
FT BINDING 162
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 163
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 257
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 311
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P20711"
SQ SEQUENCE 497 AA; 55162 MW; D65FB31F5E8D05A4 CRC64;
MEGVGGGGGG EEWLRPMDAE QLRECGHRMV DFVADYYKSI EAFPVLSQVQ PGYLKEVLPD
SAPRQPDTLD SLFDDIQQKI IPGVTHWQSP NYFAYYPSNS STAGFLGEML SAAFNIVGFS
WITSPAATEL EVIVLDWFAK MLQLPSQFLS TALGGGVIQG TASEAVLVAL LAARDRALKK
HGKHSLEKLV VYASDQTHSA LQKACQIAGI FSENVRVVIA DCNKNYAVAP EAVSEALSID
LSSGLIPFFI CATVGTTSSS AVDPLPELGQ IAKSNDMWFH IDAAYAGSAC ICPEYRHHLN
GVEEADSFNM NAHKWFLTNF DCSLLWVKDR SFLIQSLSTN PEFLKNKASQ ANSVVDFKDW
QIPLGRRFRS LKLWMVLRLY GVDNLQSYIR KHIHLAEHFE QLLLSDSRFE VVTPRTFSLV
CFRLVPPTSD HENGRKLNYD MMDGVNSSGK IFLSHTVLSG KFVLRFAVGA PLTEERHVDA
AWKLLRDEAT KVLGKMV
