DMR6_ARATH
ID DMR6_ARATH Reviewed; 341 AA.
AC Q9FLV0; Q8LEJ4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein DOWNY MILDEW RESISTANCE 6 {ECO:0000303|PubMed:15986928};
DE Short=AtDMR6 {ECO:0000303|PubMed:15986928};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=2-oxoglutarate (2OG)-Fe(II) oxygenase-like protein DMR6 {ECO:0000303|PubMed:18248595};
DE AltName: Full=Salicylate 3-hydroxylase DMR6 {ECO:0000305};
DE Short=S3H DMR6 {ECO:0000305};
DE Short=SA 3-hydroxylase DMR6 {ECO:0000305};
DE Short=Salicylic acid 3-hydroxylase DMR6 {ECO:0000305};
DE EC=1.14.13.- {ECO:0000250|UniProtKB:Q9ZSA8};
GN Name=DMR6 {ECO:0000303|PubMed:15986928};
GN OrderedLocusNames=At5g24530 {ECO:0000312|Araport:AT5G24530};
GN ORFNames=K18P6.6 {ECO:0000312|EMBL:AAK62420.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15986928; DOI=10.1094/mpmi-18-0583;
RA Van Damme M., Andel A., Huibers R.P., Panstruga R., Weisbeek P.J.,
RA Van den Ackerveken G.;
RT "Identification of arabidopsis loci required for susceptibility to the
RT downy mildew pathogen Hyaloperonospora parasitica.";
RL Mol. Plant Microbe Interact. 18:583-592(2005).
RN [6]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), MUTAGENESIS OF HIS-212 AND
RP HIS-269, DISRUPTION PHENOTYPE, AND INDUCTION BY HYALOPERONOSPORA
RP ARABIDOPSIDIS AND BTH.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija-4;
RX PubMed=18248595; DOI=10.1111/j.1365-313x.2008.03427.x;
RA van Damme M., Huibers R.P., Elberse J., Van den Ackerveken G.;
RT "Arabidopsis DMR6 encodes a putative 2OG-Fe(II) oxygenase that is defense-
RT associated but required for susceptibility to downy mildew.";
RL Plant J. 54:785-793(2008).
RN [7]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE, MUTAGENESIS
RP OF HIS-212 AND HIS-269, INDUCTION BY PATHOGENS, AND GENE FAMILY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=25376907; DOI=10.1111/tpj.12719;
RA Zeilmaker T., Ludwig N.R., Elberse J., Seidl M.F., Berke L., Van Doorn A.,
RA Schuurink R.C., Snel B., Van den Ackerveken G.;
RT "DOWNY MILDEW RESISTANT 6 and DMR6-LIKE OXYGENASE 1 are partially redundant
RT but distinct suppressors of immunity in Arabidopsis.";
RL Plant J. 81:210-222(2015).
CC -!- FUNCTION: Converts salicylic acid (SA) to 2,3-dihydroxybenzoic acid
CC (2,3-DHBA) (By similarity). Suppressor of immunity. Regulates
CC negatively defense associated genes expression (e.g. PR-1, PR-2, and
CC PR-5) (PubMed:18248595, PubMed:25376907). Negative regulator of defense
CC against Hyaloperonospora arabidopsidis (PubMed:25376907).
CC {ECO:0000250|UniProtKB:Q9ZSA8, ECO:0000269|PubMed:18248595,
CC ECO:0000269|PubMed:25376907}.
CC -!- FUNCTION: (Microbial infection) Required for susceptibility to the
CC downy mildew pathogen Hyaloperonospora arabidopsidis.
CC {ECO:0000269|PubMed:15986928, ECO:0000269|PubMed:18248595,
CC ECO:0000269|PubMed:25376907}.
CC -!- FUNCTION: (Microbial infection) Required for susceptibility to
CC Pseudomonas syringae pv. tomato DC3000. {ECO:0000269|PubMed:25376907}.
CC -!- FUNCTION: (Microbial infection) Required for susceptibility to the
CC oomycete Phytophthora capsici. {ECO:0000269|PubMed:25376907}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + salicylate = 2,3-dihydroxybenzoate + H2O +
CC NAD(+); Xref=Rhea:RHEA:51792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:30762, ChEBI:CHEBI:36654,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:Q9ZSA8};
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 -!- INDUCTION: Locally induced during infections with both compatible and
CC incompatible Hyaloperonospora arabidopsidis isolates, specifically in
CC cells containing haustoria or directly surrounding the intercellular
CC hyphae (PubMed:18248595, PubMed:25376907). Induced by the salicylic
CC acid analog BTH. Accumulates in constitutive defense mutants (e.g. sid2
CC and npr1 mutants) (PubMed:18248595). Accumulates upon infection with
CC the downy mildew Hyaloperonospora arabidopsidis, the powdery mildew
CC Erysiphe orontii, and the bacterium Pseudomonas syringae as well as
CC salicylic acid (SA) treatment (PubMed:25376907).
CC {ECO:0000269|PubMed:18248595, ECO:0000269|PubMed:25376907}.
CC -!- DISRUPTION PHENOTYPE: In the double mutant eds1-2 dmr6-1 and in dmr6-2,
CC reduced susceptibility to the downy mildew pathogen Hyaloperonospora
CC arabidopsidis (PubMed:15986928, PubMed:18248595, PubMed:25376907).
CC Reduced hyphal growth due to immature haustoria, often with aberrant
CC shapes (PubMed:15986928, PubMed:18248595). Reduced susceptibility to
CC Pseudomonas syringae pv. tomato DC3000 and the oomycete Phytophthora
CC capsici, associated with enhanced defense gene expression and elevated
CC salicylic acid levels (PubMed:25376907). Normal susceptibility to P.
CC syringae pv. tomato and Golovinomyces orontii (PubMed:15986928).
CC Enhanced expression of a subset of defense-associated genes
CC (PubMed:18248595). {ECO:0000269|PubMed:15986928,
CC ECO:0000269|PubMed:18248595, ECO:0000269|PubMed:25376907}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB010068; BAB11205.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93322.1; -; Genomic_DNA.
DR EMBL; AF386975; AAK62420.1; -; mRNA.
DR EMBL; AY081455; AAM10017.1; -; mRNA.
DR EMBL; AY085392; AAM62620.1; -; mRNA.
DR RefSeq; NP_197841.1; NM_122361.4.
DR AlphaFoldDB; Q9FLV0; -.
DR SMR; Q9FLV0; -.
DR IntAct; Q9FLV0; 1.
DR STRING; 3702.AT5G24530.1; -.
DR iPTMnet; Q9FLV0; -.
DR PaxDb; Q9FLV0; -.
DR PRIDE; Q9FLV0; -.
DR ProteomicsDB; 224289; -.
DR EnsemblPlants; AT5G24530.1; AT5G24530.1; AT5G24530.
DR GeneID; 832524; -.
DR Gramene; AT5G24530.1; AT5G24530.1; AT5G24530.
DR KEGG; ath:AT5G24530; -.
DR Araport; AT5G24530; -.
DR TAIR; locus:2153924; AT5G24530.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR InParanoid; Q9FLV0; -.
DR OMA; AKYEVVT; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9FLV0; -.
DR BioCyc; ARA:AT5G24530-MON; -.
DR PRO; PR:Q9FLV0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLV0; baseline and differential.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0033759; F:flavone synthase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034785; F:salicylate 5-hydroxylase activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IGI:TAIR.
DR GO; GO:0009620; P:response to fungus; IGI:TAIR.
DR GO; GO:0002239; P:response to oomycetes; IMP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0046244; P:salicylic acid catabolic process; ISS:UniProtKB.
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 Dioxygenase; Iron; Metal-binding; NAD; Oxidoreductase; Plant defense;
KW Reference proteome.
FT CHAIN 1..341
FT /note="Protein DOWNY MILDEW RESISTANCE 6"
FT /id="PRO_0000435627"
FT DOMAIN 188..288
FT /note="Fe2OG dioxygenase"
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 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 279
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 212
FT /note="H->Q: Enhanced susceptibility to H. arabidopsidis."
FT /evidence="ECO:0000269|PubMed:25376907"
FT MUTAGEN 269
FT /note="H->D: Enhanced susceptibility to H. arabidopsidis."
FT /evidence="ECO:0000269|PubMed:25376907"
FT CONFLICT 68
FT /note="I -> K (in Ref. 4; AAM62620)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="H -> R (in Ref. 4; AAM62620)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="C -> F (in Ref. 4; AAM62620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 39364 MW; E3A499D08AA6850E CRC64;
MAAKLISTGF RHTTLPENYV RPISDRPRLS EVSQLEDFPL IDLSSTDRSF LIQQIHQACA
RFGFFQVINH GVNKQIIDEM VSVAREFFSM SMEEKMKLYS DDPTKTTRLS TSFNVKKEEV
NNWRDYLRLH CYPIHKYVNE WPSNPPSFKE IVSKYSREVR EVGFKIEELI SESLGLEKDY
MKKVLGEQGQ HMAVNYYPPC PEPELTYGLP AHTDPNALTI LLQDTTVCGL QILIDGQWFA
VNPHPDAFVI NIGDQLQALS NGVYKSVWHR AVTNTENPRL SVASFLCPAD CAVMSPAKPL
WEAEDDETKP VYKDFTYAEY YKKFWSRNLD QEHCLENFLN N
