ODD11_ORYSJ
ID ODD11_ORYSJ Reviewed; 357 AA.
AC Q94LP4; A0A5S6RC26; Q7G7Q9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase 11 {ECO:0000303|PubMed:25728912};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:25728912};
DE AltName: Full=Melatonin 2-hydroxylase {ECO:0000303|PubMed:25728912};
GN Name=2ODD11 {ECO:0000303|PubMed:25728912};
GN OrderedLocusNames=Os10g0558700 {ECO:0000312|EMBL:BAF27202.1},
GN LOC_Os10g40934 {ECO:0000312|EMBL:AAP54990.1};
GN ORFNames=OsJ_32437 {ECO:0000312|EMBL:EAZ16953.1},
GN OSJNBa0010C11.19 {ECO:0000312|EMBL:AAK55454.1},
GN OSJNBa0042H09.28 {ECO:0000312|EMBL:AAL79801.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=25728912; DOI=10.1111/jpi.12220;
RA Byeon Y., Back K.;
RT "Molecular cloning of melatonin 2-hydroxylase responsible for 2-
RT hydroxymelatonin production in rice (Oryza sativa).";
RL J. Pineal Res. 58:343-351(2015).
RN [8]
RP SUBCELLULAR LOCATION, AND INDUCTION BY CADMIUM.
RX PubMed=25783167; DOI=10.1111/jpi.12232;
RA Byeon Y., Lee H.Y., Hwang O.J., Lee H.J., Lee K., Back K.;
RT "Coordinated regulation of melatonin synthesis and degradation genes in
RT rice leaves in response to cadmium treatment.";
RL J. Pineal Res. 58:470-478(2015).
CC -!- FUNCTION: Involved in melatonin degradation (PubMed:25728912).
CC Catalyzes the hydroxylation of melatonin to produce 2-hydroxymelatonin
CC (PubMed:25728912). {ECO:0000269|PubMed:25728912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + melatonin + O2 = 2-hydroxymelatonin + CO2 +
CC succinate; Xref=Rhea:RHEA:62512, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16796, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:145792;
CC Evidence={ECO:0000269|PubMed:25728912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62513;
CC Evidence={ECO:0000269|PubMed:25728912};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:25728912};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:25728912};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=371 uM for melatonin {ECO:0000269|PubMed:25728912};
CC Vmax=7.1 pmol/sec/mg enzyme toward melatonine
CC {ECO:0000269|PubMed:25728912};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:25728912};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:25728912};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25783167}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots. {ECO:0000269|PubMed:25728912}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC069300; AAK55454.1; -; Genomic_DNA.
DR EMBL; AC079874; AAL79801.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54990.1; -; Genomic_DNA.
DR EMBL; DP000086; ABG66251.1; -; Genomic_DNA.
DR EMBL; DP000086; ABG66253.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27202.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12021.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ16953.1; -; Genomic_DNA.
DR EMBL; AK067086; BAG90259.1; -; mRNA.
DR RefSeq; XP_015614185.1; XM_015758699.1.
DR RefSeq; XP_015614186.1; XM_015758700.1.
DR AlphaFoldDB; Q94LP4; -.
DR SMR; Q94LP4; -.
DR STRING; 4530.OS10T0558700-02; -.
DR PRIDE; Q94LP4; -.
DR EnsemblPlants; Os10t0558700-02; Os10t0558700-02; Os10g0558700.
DR GeneID; 112935986; -.
DR Gramene; Os10t0558700-02; Os10t0558700-02; Os10g0558700.
DR KEGG; osa:4349363; -.
DR eggNOG; KOG0143; Eukaryota.
DR InParanoid; Q94LP4; -.
DR OMA; HYPCENI; -.
DR OrthoDB; 1005149at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q94LP4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..357
FT /note="2-oxoglutarate-dependent dioxygenase 11"
FT /id="PRO_0000449518"
FT DOMAIN 207..307
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 298
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 357 AA; 40280 MW; 7BC21F690AB7484C CRC64;
MAGARSVGSL PVPNVQALAE ICNDPDEHIP ERYIRPEASS EEVINNYQGD MAIPIIDLKK
LLCPQSSEEE CVKLRSACQY WGFFLLINHG VPDEVIANLK RDIVDFFSQP LDTKKEYTQL
PNSLEGYGQS FVFSEDQKLD WADMLYLHVH PSDSRDLRFW PTSPASFRQS IDAYSSETKS
LALCLFEFMA KAVGAKPESL LDLFEEQPRG LRMAYYPPCR QADKVMGLSP HSDAGGLTLL
LEINNVQGLQ IKKDGKWFSI DAPNGALIAN IGDTLEILSN GKFRSVEHRA VINPNKERIS
AALFHYPSEN MVISPLPEFV KDGKVKYRSI SYLDFMKQIF TQQLDGKNRV EVLKLDQ
