DAO_ORYSJ
ID DAO_ORYSJ Reviewed; 300 AA.
AC Q7XKU5; A0A0P0WBR1;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase DAO;
DE EC=1.14.11.-;
DE AltName: Full=Protein DIOXYGENASE FOR AUXIN OXIDATION;
GN Name=DAO; OrderedLocusNames=Os04g0475600, LOC_Os04g39980;
GN ORFNames=OSJNBa0022H21.12;
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 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24094741; DOI=10.1016/j.devcel.2013.09.005;
RA Zhao Z., Zhang Y., Liu X., Zhang X., Liu S., Yu X., Ren Y., Zheng X.,
RA Zhou K., Jiang L., Guo X., Gai Y., Wu C., Zhai H., Wang H., Wan J.;
RT "A role for a dioxygenase in auxin metabolism and reproductive development
RT in rice.";
RL Dev. Cell 27:113-122(2013).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase essential for auxin
CC catabolism and maintenance of auxin homeostasis in reproductive organs.
CC Catalyzes the irreversible oxidation of indole-3-acetic acid (IAA) to
CC the biologically inactive 2-oxoindole-3-acetic acid (OxIAA).
CC {ECO:0000269|PubMed:24094741}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- DISRUPTION PHENOTYPE: Male sterility and production of parthenocarpic
CC seeds. Increased levels of free IAA in anthers and ovaries.
CC {ECO:0000269|PubMed:24094741}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AL731582; CAE05492.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14989.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89685.1; -; Genomic_DNA.
DR EMBL; AK105400; BAG97226.1; -; mRNA.
DR EMBL; AK121520; BAH00532.1; -; mRNA.
DR RefSeq; XP_015633778.1; XM_015778292.1.
DR PDB; 6KUN; X-ray; 2.00 A; A/B=1-300.
DR PDBsum; 6KUN; -.
DR AlphaFoldDB; Q7XKU5; -.
DR SMR; Q7XKU5; -.
DR STRING; 4530.OS04T0475600-01; -.
DR PaxDb; Q7XKU5; -.
DR PRIDE; Q7XKU5; -.
DR EnsemblPlants; Os04t0475600-01; Os04t0475600-01; Os04g0475600.
DR GeneID; 4336150; -.
DR Gramene; Os04t0475600-01; Os04t0475600-01; Os04g0475600.
DR KEGG; osa:4336150; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_3_2_1; -.
DR InParanoid; Q7XKU5; -.
DR OMA; CKEATVR; -.
DR OrthoDB; 622449at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XKU5; OS.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009852; P:auxin catabolic process; IMP:UniProtKB.
DR GO; GO:0010252; P:auxin homeostasis; IBA:GO_Central.
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 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..300
FT /note="2-oxoglutarate-dependent dioxygenase DAO"
FT /id="PRO_0000424610"
FT DOMAIN 149..252
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 242
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 300 AA; 32102 MW; 195F0D4B98399D02 CRC64;
MVEIPAIDLR LAGGGGGAEE TARLRDACAR LGCFRVSGHG VPPGLQAEMK AAVRALFDLP
DDAKRRNADI IPGSGYVPPG TANPLYEAFG LCDAAAPADV DAFCARLDAP PHVRETVKAY
AERMHSLIVD VAGKVAASLG LHGASFQDWP CQFRMNRYNY TQDSVGSPGV QVHTDSGFLT
VLQEDECVGG LEVLDPAAGE FVPVDPLPGS FVVNVGDVGQ AWSNGRLHNV KHRVQCVAAV
PRVSIAMFLL APKDDTVSAP GELVDGEHPR RYREFKYDDY RRLRLSTGER AGEALARLAA
