DLO2_ARATH
ID DLO2_ARATH Reviewed; 348 AA.
AC Q9ZSA7;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein DMR6-LIKE OXYGENASE 2 {ECO:0000303|PubMed:25376907};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=2-oxoglutarate (2OG)-Fe(II) oxygenase-like protein DLO2 {ECO:0000303|PubMed:25376907};
DE AltName: Full=Salicylate 3-hydroxylase DLO2 {ECO:0000305};
DE Short=S3H DLO2 {ECO:0000305};
DE Short=SA 3-hydroxylase DLO2 {ECO:0000305};
DE Short=Salicylic acid 3-hydroxylase DLO2 {ECO:0000305};
DE EC=1.14.13.- {ECO:0000250|UniProtKB:Q9ZSA8};
GN Name=DLO2 {ECO:0000303|PubMed:25376907};
GN OrderedLocusNames=At4g10490 {ECO:0000312|Araport:AT4G10490};
GN ORFNames=F3H7.17 {ECO:0000312|EMBL:AAD03424.1},
GN F7L13.70 {ECO:0000312|EMBL:CAB40042.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION, FUNCTION (MICROBIAL INFECTION), 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). Negative regulator of defense against
CC Hyaloperonospora arabidopsidis (PubMed:25376907).
CC {ECO:0000250|UniProtKB:Q9ZSA8, ECO:0000269|PubMed:25376907}.
CC -!- FUNCTION: (Microbial infection) Confers susceptibility to the downy
CC mildew pathogen Hyaloperonospora arabidopsidis.
CC {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 -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF118222; AAD03424.1; -; Genomic_DNA.
DR EMBL; AL049524; CAB40042.1; -; Genomic_DNA.
DR EMBL; AL161517; CAB78172.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82890.1; -; Genomic_DNA.
DR EMBL; BT003944; AAO41989.1; -; mRNA.
DR EMBL; BT005030; AAO50563.1; -; mRNA.
DR PIR; T04184; T04184.
DR RefSeq; NP_192787.1; NM_117117.3.
DR AlphaFoldDB; Q9ZSA7; -.
DR SMR; Q9ZSA7; -.
DR STRING; 3702.AT4G10490.1; -.
DR PaxDb; Q9ZSA7; -.
DR PRIDE; Q9ZSA7; -.
DR ProteomicsDB; 224288; -.
DR EnsemblPlants; AT4G10490.1; AT4G10490.1; AT4G10490.
DR GeneID; 826641; -.
DR Gramene; AT4G10490.1; AT4G10490.1; AT4G10490.
DR KEGG; ath:AT4G10490; -.
DR Araport; AT4G10490; -.
DR TAIR; locus:2127686; AT4G10490.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9ZSA7; -.
DR OMA; RDACMNV; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9ZSA7; -.
DR BioCyc; ARA:AT4G10490-MON; -.
DR PRO; PR:Q9ZSA7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSA7; baseline and differential.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002229; P:defense response to oomycetes; IMP: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 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; NAD; Oxidoreductase; Plant defense;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Protein DMR6-LIKE OXYGENASE 2"
FT /id="PRO_0000435629"
FT DOMAIN 194..294
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 285
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 348 AA; 39282 MW; 15290E7649C680D2 CRC64;
MAASKLLVSD IASVVDHVPS NYVRPVSDRP KMSEVQTSGD SIPLIDLHDL HGPNRADIIN
QFAHACSSCG FFQIKNHGVP EETIKKMMNA AREFFRQSES ERVKHYSADT KKTTRLSTSF
NVSKEKVSNW RDFLRLHCYP IEDFINEWPS TPISFREVTA EYATSVRALV LTLLEAISES
LGLAKDRVSN TIGKHGQHMA INYYPRCPQP ELTYGLPGHK DANLITVLLQ DEVSGLQVFK
DGKWIAVNPV PNTFIVNLGD QMQVISNEKY KSVLHRAVVN SDMERISIPT FYCPSEDAVI
SPAQELINEE EDSPAIYRNF TYAEYFEKFW DTAFDTESCI DSFKASTA
