ODD19_ORYSJ
ID ODD19_ORYSJ Reviewed; 337 AA.
AC Q6Z244; A0A0P0XHE5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase 19 {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=2ODD19 {ECO:0000303|PubMed:25728912};
GN OrderedLocusNames=Os08g0480200 {ECO:0000312|EMBL:BAF23972.1},
GN LOC_Os08g37456 {ECO:0000305};
GN ORFNames=OJ1113_A10.32 {ECO:0000312|EMBL:BAD09760.1},
GN OSJNBb0092C08.2 {ECO:0000312|EMBL:BAD10270.1};
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, 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=302 uM for melatonin {ECO:0000269|PubMed:25728912};
CC Vmax=9.3 pmol/sec/mg enzyme toward melatonine
CC {ECO:0000269|PubMed:25728912};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:25728912};
CC Temperature dependence:
CC Optimum temperature is 45 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 -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:25783167}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AP004643; BAD09760.1; -; Genomic_DNA.
DR EMBL; AP005391; BAD10270.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23972.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05916.1; -; Genomic_DNA.
DR EMBL; AK065790; BAG89680.1; -; mRNA.
DR RefSeq; XP_015648666.1; XM_015793180.1.
DR AlphaFoldDB; Q6Z244; -.
DR SMR; Q6Z244; -.
DR STRING; 4530.OS08T0480200-01; -.
DR PaxDb; Q6Z244; -.
DR PRIDE; Q6Z244; -.
DR EnsemblPlants; Os08t0480200-01; Os08t0480200-01; Os08g0480200.
DR GeneID; 4345848; -.
DR Gramene; Os08t0480200-01; Os08t0480200-01; Os08g0480200.
DR KEGG; osa:4345848; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR InParanoid; Q6Z244; -.
DR OMA; NGHETEV; -.
DR OrthoDB; 1005149at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
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..337
FT /note="2-oxoglutarate-dependent dioxygenase 19"
FT /id="PRO_0000449519"
FT DOMAIN 179..283
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 274
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 337 AA; 36999 MW; AD9614061DD54796 CRC64;
MVAPSRLPSH EEQSAAAAAD GSATPSQGIP VVDLGVLING AADERSRAIR DLGRACEDWG
FFMVTNHGVP EALREAIMDA CKELFRLPLE EKKEYMRAKP MDPIRIGTGF YSVVDAVPCR
RDYLKMFSHP EFHCPEKPAK LREIATEYAT CTRALLLELT KAISESLGLA GGRLSEALNL
ESCFQILVGN HYPACSRPDE QAMGLSAHSD HGLLTLLFQN GVDGLQVKHD GEWLLAKPLP
GSFFVIAGDQ LEIVTNGRYK GVLHRAVVGG EQSRMSFVSL IGPCMDTVVE PLPEMAADGR
GLEFRGIRYR DYMEMQQSNS INEKTALDIV RVMHQAG
