ODD33_ORYSJ
ID ODD33_ORYSJ Reviewed; 328 AA.
AC Q6K332; A0A0P0XIU3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase 33 {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=2ODD33 {ECO:0000303|PubMed:25728912};
GN OrderedLocusNames=Os09g0245500 {ECO:0000312|EMBL:BAF24572.1},
GN LOC_Os09g07020 {ECO:0000305};
GN ORFNames=OJ1058_F03.5 {ECO:0000312|EMBL:BAD23370.1},
GN OsJ_28501 {ECO:0000312|EMBL:EEE69249.1},
GN OSJNBa0069P02.20 {ECO:0000312|EMBL:BAD23538.1};
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 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 [5]
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 [6]
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=121 uM for melatonin {ECO:0000269|PubMed:25728912};
CC Vmax=1.7 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 roots and shoots.
CC {ECO:0000269|PubMed:25728912}.
CC -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:25783167}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT07007.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005550; BAD23370.1; -; Genomic_DNA.
DR EMBL; AP005729; BAD23538.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24572.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT07007.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000146; EEE69249.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6K332; -.
DR SMR; Q6K332; -.
DR STRING; 4530.OS09T0245500-01; -.
DR EnsemblPlants; Os09t0245500-01; Os09t0245500-01; Os09g0245500.
DR Gramene; Os09t0245500-01; Os09t0245500-01; Os09g0245500.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_0_1; -.
DR InParanoid; Q6K332; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
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..328
FT /note="2-oxoglutarate-dependent dioxygenase 33"
FT /id="PRO_0000449521"
FT DOMAIN 182..287
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 278
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 328 AA; 36835 MW; 6B0DF323848908D0 CRC64;
MGSDFKAIPL IDISPLVGKI DDPSMVNDED LLQVVQMLDD ACREAGFFYV KGHGIADSLM
KQVRDVTQKF FQLPYEEKLK IKMTPQSGYR GYQRVGENIT KGKPDMHEAI DCYTPIEPGK
YGDLAKPMVG SNLWPKYPSN FDVLLENYIS LLRDLSRKIM RGIALALGAP VDAFEGTTAG
DPFWVCRLIG YPVSTDIPEE QRTDTGCGAH TDYGLLTLVN QDDDICALEV RNQSGEWIYA
KPIPGTFVCN IGDMLKVWSN GIYQPTLHRV VNNSPRYRVS VAFFYESNFD AAVEPVEFCR
ERTGGVAKYE KVVYGEHLVQ KVLTNFVM
