AOP3C_ARATH
ID AOP3C_ARATH Reviewed; 411 AA.
AC Q9ZTA1; F4JHY7; F4JHY8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase AOP3;
DE EC=1.14.11.-;
GN Name=AOP3; OrderedLocusNames=At4g03050; ORFNames=T4I9.7;
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 GENE FAMILY, AND LACK OF TISSUE SPECIFICITY.
RX PubMed=11251105; DOI=10.2307/3871415;
RA Kliebenstein D.J., Lambrix V.M., Reichelt M., Gershenzon J.,
RA Mitchell-Olds T.;
RT "Gene duplication in the diversification of secondary metabolism: tandem 2-
RT oxoglutarate-dependent dioxygenases control glucosinolate biosynthesis in
RT Arabidopsis.";
RL Plant Cell 13:681-693(2001).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in
CC glucosinolates biosynthesis. Catalyzes the conversion of
CC methylsulfinylalkyl glucosinolates to hydroxyalkyl glucosinolates (By
CC similarity). {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZTA1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Not expressed.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- CAUTION: AOP1, AOP2 and AOP3 are found in tandem and inverted
CC duplications on chromosome IV and encode 2-oxoglutarate-dependent
CC dioxygenases involved in glucosinolates biosynthesis. In cv. Columbia,
CC AOP2 (AC Q9ZTA2) cDNA contains a 5-bp deletion that leads to a non-
CC functional protein and AOP3 (AC Q9ZTA1) is not expressed. The
CC functional and expressed alleles for AOP2 (AC Q945B5) and AOP3 (AC
CC Q945B4) are found in cv. Cvi and cv. Landsberg erecta, respectively. No
CC ecotype coexpresses both AOP2 and AOP3 genes. The catalytic role of
CC AOP1 is still uncertain (PubMed:11251105).
CC {ECO:0000305|PubMed:11251105}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF069442; AAC79100.1; -; Genomic_DNA.
DR EMBL; AL161495; CAB77790.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82265.2; -; Genomic_DNA.
DR EMBL; CP002687; AEE82266.2; -; Genomic_DNA.
DR PIR; T01388; T01388.
DR RefSeq; NP_001319854.1; NM_001340416.1. [Q9ZTA1-1]
DR RefSeq; NP_001319855.1; NM_001340417.1. [Q9ZTA1-1]
DR AlphaFoldDB; Q9ZTA1; -.
DR SMR; Q9ZTA1; -.
DR STRING; 3702.AT4G03050.2; -.
DR PaxDb; Q9ZTA1; -.
DR PRIDE; Q9ZTA1; -.
DR ProteomicsDB; 244993; -. [Q9ZTA1-1]
DR EnsemblPlants; AT4G03050.1; AT4G03050.1; AT4G03050. [Q9ZTA1-1]
DR EnsemblPlants; AT4G03050.2; AT4G03050.2; AT4G03050. [Q9ZTA1-1]
DR GeneID; 828104; -.
DR Gramene; AT4G03050.1; AT4G03050.1; AT4G03050. [Q9ZTA1-1]
DR Gramene; AT4G03050.2; AT4G03050.2; AT4G03050. [Q9ZTA1-1]
DR KEGG; ath:AT4G03050; -.
DR Araport; AT4G03050; -.
DR TAIR; locus:2139370; AT4G03050.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_3_0_1; -.
DR OMA; LMNGRIP; -.
DR OrthoDB; 830141at2759; -.
DR PhylomeDB; Q9ZTA1; -.
DR BioCyc; MetaCyc:AT4G03050-MON; -.
DR PRO; PR:Q9ZTA1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZTA1; baseline and differential.
DR Genevisible; Q9ZTA1; AT.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR Gene3D; 2.60.120.330; -; 2.
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 Alternative splicing; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..411
FT /note="2-oxoglutarate-dependent dioxygenase AOP3"
FT /id="PRO_0000423937"
FT DOMAIN 259..356
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 279
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 336
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 347
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 411 AA; 44963 MW; 2B440CA2C7E0BB31 CRC64;
MGSCSPQLPL ICLSDQTLKP GSSKWVKVRS DVRKALEDYG CFEAKIDQVS MELQGSVLKA
MQELFALPTE AKQRNVCPKP FTGYLSHNGL SESFGIKDAN ILEKAHEFTQ QLWPEGNKSI
SKMIQLYAEK LAELDMMVRR LILESYGIEY FIDEHLNSTY YRMRLMKYIA RPDNDITAAV
GANVDNGAND NADGDANVND DGASIGVKVN VDVGDDVNDN DSVNIGVGVD INVETNVNGD
LDAEANGDAT AWVVGAVSGN ASVGAKEANV DAELGLPSHT DKSLTGIIYQ HQIDGLEVKT
KEGKWIRVKP APNTVIVIAG DALCALMNGR IPSPYHRVRV TEKKKTRYAA ALFSNPKEGY
IIDSPKELVD EKHPRAFKPF DFVDLFNFYH TEAGRRAPST LQAFCGVSAG K
