ODD21_ORYSJ
ID ODD21_ORYSJ Reviewed; 333 AA.
AC Q7XR83; A0A0N7KJW1; Q259W6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase 21, chloroplastic {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};
DE AltName: Full=OsSTA135 {ECO:0000305};
DE Flags: Precursor;
GN Name=2ODD21 {ECO:0000303|PubMed:25728912}; Synonyms=STA135 {ECO:0000305};
GN OrderedLocusNames=Os04g0667400 {ECO:0000312|EMBL:BAF16100.1},
GN LOC_Os04g57180 {ECO:0000305};
GN ORFNames=B0811B10.4 {ECO:0000312|EMBL:CAJ86195.1},
GN OsJ_16545 {ECO:0000312|EMBL:EEE61866.1},
GN OSJNBa0043A12.2 {ECO:0000312|EMBL:CAE02797.1};
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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 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 [7]
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=145 uM for melatonin {ECO:0000269|PubMed:25728912};
CC Vmax=18.5 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: Plastid, chloroplast
CC {ECO:0000269|PubMed:25783167}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {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=CAJ86195.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606619; CAE02797.1; -; Genomic_DNA.
DR EMBL; AL732340; CAJ86195.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF16100.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91521.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61866.1; -; Genomic_DNA.
DR RefSeq; XP_015634218.1; XM_015778732.1.
DR AlphaFoldDB; Q7XR83; -.
DR SMR; Q7XR83; -.
DR STRING; 4530.OS04T0667400-01; -.
DR PaxDb; Q7XR83; -.
DR PRIDE; Q7XR83; -.
DR EnsemblPlants; Os04t0667400-01; Os04t0667400-01; Os04g0667400.
DR GeneID; 4337327; -.
DR Gramene; Os04t0667400-01; Os04t0667400-01; Os04g0667400.
DR KEGG; osa:4337327; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR InParanoid; Q7XR83; -.
DR OMA; GTYAVEM; -.
DR OrthoDB; 830141at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; 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 Chloroplast; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide; Vitamin C.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..333
FT /note="2-oxoglutarate-dependent dioxygenase 21,
FT chloroplastic"
FT /id="PRO_0000449520"
FT DOMAIN 180..281
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 272
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 333 AA; 37187 MW; 10D5F707B029FEBE CRC64;
MPAVAGSLYM ASQHKGVPPP LPPPPRPLPV INLGRLTMDS ASRALAVRDI VLACRERGCF
EVVNHGISRS CMNGALEAAS EFFQLSTERK EEFASDDIRQ PIRYDTSSRD GISMSRSFLK
HYANPLDDWI KFWPTQPPTY REKMGEYAVE TQRVSMQLME AILQGLGLGP SYLQEKLEGG
VQFVALNNYP QSSAKKADKI GLAPHSDYGF LTILLQSSPG LEVMHHEDDA WTSVPAIPGA
LHVHVGDHLE VLSNGQLKSL VHRAVLNPNE SRISIASIHG LSMDEEVHCA EELVDEHHPK
MYRGSSFQDF LDFLPANMNR YKRYVESLRI DKP
