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THT1_ORYSJ
ID   THT1_ORYSJ              Reviewed;         436 AA.
AC   Q338X7;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Tryptamine hydroxycinnamoyltransferase 1 {ECO:0000305};
DE            Short=OsTHT1 {ECO:0000303|PubMed:27354554};
DE            EC=2.3.1.- {ECO:0000305};
GN   Name=THT1 {ECO:0000303|PubMed:27354554};
GN   OrderedLocusNames=Os10g0379100 {ECO:0000312|EMBL:BAT10617.1},
GN   LOC_Os10g23310 {ECO:0000312|EMBL:ABB47405.1};
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=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=27354554; DOI=10.1105/tpc.16.00265;
RA   Peng M., Gao Y., Chen W., Wang W., Shen S., Shi J., Wang C., Zhang Y.,
RA   Zou L., Wang S., Wan J., Liu X., Gong L., Luo J.;
RT   "Evolutionarily distinct BAHD N-acyltransferases are responsible for
RT   natural variation of aromatic amine conjugates in rice.";
RL   Plant Cell 28:1533-1550(2016).
CC   -!- FUNCTION: Hydroxycinnamoyl transferase that catalyzes the transfer of
CC       an acyl from p-coumaryol-CoA to tryptamine, to produce coumaroyl
CC       tryptamine. Serotonin, tyramine, and to a lesser extent agmatine, serve
CC       as acyl acceptors in vitro. Can use caffeoyl-CoA, and to a lesser
CC       extent benzoyl-CoA, as acyl donors. {ECO:0000269|PubMed:27354554}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=91.4 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:27354554};
CC         KM=138.9 uM for caffeoyl-CoA {ECO:0000269|PubMed:27354554};
CC         KM=369.9 uM for benzoyl-CoA {ECO:0000269|PubMed:27354554};
CC         KM=82 uM for tryptamine {ECO:0000269|PubMed:27354554};
CC         KM=112.9 uM for serotonin {ECO:0000269|PubMed:27354554};
CC         KM=178 uM for tyramine {ECO:0000269|PubMed:27354554};
CC         KM=1489 uM for agmatine {ECO:0000269|PubMed:27354554};
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; DP000086; ABB47405.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF26398.1; -; Genomic_DNA.
DR   EMBL; AP014966; BAT10617.1; -; Genomic_DNA.
DR   RefSeq; XP_015613139.1; XM_015757653.1.
DR   AlphaFoldDB; Q338X7; -.
DR   SMR; Q338X7; -.
DR   STRING; 4530.OS10T0379100-01; -.
DR   PaxDb; Q338X7; -.
DR   PRIDE; Q338X7; -.
DR   EnsemblPlants; Os10t0379100-01; Os10t0379100-01; Os10g0379100.
DR   GeneID; 4348503; -.
DR   Gramene; Os10t0379100-01; Os10t0379100-01; Os10g0379100.
DR   KEGG; osa:4348503; -.
DR   eggNOG; ENOG502QVP8; Eukaryota.
DR   HOGENOM; CLU_014546_6_2_1; -.
DR   InParanoid; Q338X7; -.
DR   OMA; IPTMFAW; -.
DR   OrthoDB; 1130893at2759; -.
DR   SABIO-RK; Q338X7; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   ExpressionAtlas; Q338X7; baseline and differential.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR   GO; GO:0050734; F:hydroxycinnamoyltransferase activity; IDA:UniProtKB.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..436
FT                   /note="Tryptamine hydroxycinnamoyltransferase 1"
FT                   /id="PRO_0000437766"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ   SEQUENCE   436 AA;  46726 MW;  B62FBB7A972F4459 CRC64;
     MAAVTVEITR SEVLRPSPAS AGGGEMVPLT VFDRAATDGY IPTMFAWDAA AAAALSNDAI
     KDGLAAVLSR FPHLAGRFAV DERGRKCFRL NNAGARVLEA SAAGDLADAL AHDVAAHVNQ
     LYPQADKDRV DEPLLQVQLT RYTCGGLVIG AVSHHQVADG QSMSVFFTEW AAAVRTAGAA
     LPTPFLDRSA VAAPRIPPAP AFDHRNVEFR GEGSRSHSYG ALPLERMRNL AVHFPPEFVA
     GLKARVGGAR CSTFQCLLAH AWKKITAARD LSPKEYTQVR VAVNCRGRAG PAVPTDYFGN
     MVLWAFPRMQ VRDLLSASYA AVVGVIRDAV ARVDERYIQS FVDFGEVAAG DELAPTAAEP
     GTAFCPDLEV DSWIGFRFHD LDFGGGPPCA FLPPDVPIDG LLIFVPSCAA KGGVEMFMAL
     DDQHVEALRQ ICYSMD
 
 
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