DLO1_ARATH
ID DLO1_ARATH Reviewed; 349 AA.
AC Q9ZSA8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein DMR6-LIKE OXYGENASE 1 {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 DLO1 {ECO:0000303|PubMed:25376907};
DE AltName: Full=Protein SENESCENCE-ASSOCIATED GENE 108 {ECO:0000303|PubMed:23959884};
DE AltName: Full=Salicylate 3-hydroxylase DLO1 {ECO:0000303|PubMed:23959884};
DE Short=S3H DLO1 {ECO:0000303|PubMed:23959884};
DE Short=SA 3-hydroxylase DLO1 {ECO:0000303|PubMed:23959884};
DE Short=Salicylic acid 3-hydroxylase DLO1 {ECO:0000303|PubMed:23959884};
DE EC=1.14.13.- {ECO:0000269|PubMed:23959884};
GN Name=DLO1 {ECO:0000303|PubMed:25376907};
GN Synonyms=SAG108 {ECO:0000303|PubMed:23959884};
GN OrderedLocusNames=At4g10500 {ECO:0000312|Araport:AT4G10500};
GN ORFNames=F3H7.16 {ECO:0000312|EMBL:AAD03425.1},
GN F7L13.80 {ECO:0000312|EMBL:CAB40043.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY ERYSIPHE CICHORACEARUM.
RX PubMed=12920300; DOI=10.1126/science.1086716;
RA Nishimura M.T., Stein M., Hou B.-H., Vogel J.P., Edwards H.,
RA Somerville S.C.;
RT "Loss of a callose synthase results in salicylic acid-dependent disease
RT resistance.";
RL Science 301:969-972(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY SENESCENCE AND SALICYLIC
RP ACID.
RC STRAIN=cv. Columbia;
RX PubMed=23959884; DOI=10.1073/pnas.1302702110;
RA Zhang K., Halitschke R., Yin C., Liu C.J., Gan S.S.;
RT "Salicylic acid 3-hydroxylase regulates Arabidopsis leaf longevity by
RT mediating salicylic acid catabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14807-14812(2013).
RN [7]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), INDUCTION BY PATHOGENS, AND GENE
RP 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 both 2,3-dihydroxybenzoic
CC acid (2,3-DHBA) and 2,5-DHBA in vitro but only 2,3-DHBA in vivo.
CC Component of a negative feedback regulation system of SA levels during
CC senescence. Regulates both onset and progression of leaf senescence
CC (PubMed:23959884). Negative regulator of defense against
CC Hyaloperonospora arabidopsidis (PubMed:25376907).
CC {ECO:0000269|PubMed:23959884, 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:0000269|PubMed:23959884};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:23959884};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58.29 uM for salicylic acid (at pH 6.0 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:23959884};
CC Vmax=498 nmol/min/mg enzyme with salicylic acid as substrate (at pH
CC 6.0 and 40 degrees Celsius) {ECO:0000269|PubMed:23959884};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:23959884};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:23959884};
CC -!- INDUCTION: Induced by the powdery mildew pathogen Erysiphe
CC cichoracearum (PubMed:12920300). Accumulates upon infection with the
CC downy mildew Hyaloperonospora arabidopsidis, the powdery mildew
CC Erysiphe orontii, and the bacterium Pseudomonas syringae. Present only
CC in or around the main veins of cotyledons and leaves infected by H.
CC arabidopsidis (PubMed:25376907). Induced by salicylic acid (SA)
CC (PubMed:23959884, PubMed:25376907). Accumulates in senescing leaves
CC (PubMed:23959884). {ECO:0000269|PubMed:12920300,
CC ECO:0000269|PubMed:23959884, ECO:0000269|PubMed:25376907}.
CC -!- DISRUPTION PHENOTYPE: Impaired production of 2,3-DHBA sugar conjugates
CC but accumulation of salicylic acid (SA) and its sugar conjugates.
CC Precocious senescence. Enhanced expression of senescence-associated and
CC defense-related genes. {ECO:0000269|PubMed:23959884}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF118222; AAD03425.1; -; Genomic_DNA.
DR EMBL; AL049524; CAB40043.1; -; Genomic_DNA.
DR EMBL; AL161517; CAB78173.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82891.1; -; Genomic_DNA.
DR EMBL; BT010537; AAQ65160.1; -; mRNA.
DR EMBL; AK176678; BAD44441.1; -; mRNA.
DR EMBL; AK176911; BAD44674.1; -; mRNA.
DR PIR; T04185; T04185.
DR RefSeq; NP_192788.1; NM_117118.5.
DR AlphaFoldDB; Q9ZSA8; -.
DR SMR; Q9ZSA8; -.
DR IntAct; Q9ZSA8; 2.
DR STRING; 3702.AT4G10500.1; -.
DR PaxDb; Q9ZSA8; -.
DR PRIDE; Q9ZSA8; -.
DR ProteomicsDB; 222220; -.
DR EnsemblPlants; AT4G10500.1; AT4G10500.1; AT4G10500.
DR GeneID; 826642; -.
DR Gramene; AT4G10500.1; AT4G10500.1; AT4G10500.
DR KEGG; ath:AT4G10500; -.
DR Araport; AT4G10500; -.
DR TAIR; locus:2127691; AT4G10500.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9ZSA8; -.
DR OMA; VEYWDKF; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9ZSA8; -.
DR BioCyc; ARA:AT4G10500-MON; -.
DR PRO; PR:Q9ZSA8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSA8; 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:0010150; P:leaf senescence; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0002239; P:response to oomycetes; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0046244; P:salicylic acid catabolic process; IDA: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..349
FT /note="Protein DMR6-LIKE OXYGENASE 1"
FT /id="PRO_0000435628"
FT DOMAIN 197..296
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 206
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 287
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 289
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 349 AA; 39234 MW; 936403104FCA9761 CRC64;
MATSAISKLL VSDFASSVHI PSNYVRPISD RPNLSEVESS GDSIPLIDLR DLHGPNRAVI
VQQLASACST YGFFQIKNHG VPDTTVNKMQ TVAREFFHQP ESERVKHYSA DPTKTTRLST
SFNVGADKVL NWRDFLRLHC FPIEDFIEEW PSSPISFREV TAEYATSVRA LVLRLLEAIS
ESLGLESDHI SNILGKHAQH MAFNYYPPCP EPELTYGLPG HKDPTVITVL LQDQVSGLQV
FKDDKWVAVS PIPNTFIVNI GDQMQVISND KYKSVLHRAV VNTENERLSI PTFYFPSTDA
VIGPAHELVN EQDSLAIYRT YPFVEYWDKF WNRSLATASC LDAFKAPTT
