AOP1C_ARATH
ID AOP1C_ARATH Reviewed; 322 AA.
AC Q9ZTA3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable 2-oxoglutarate-dependent dioxygenase AOP1;
DE EC=1.14.11.-;
GN Name=AOP1; Synonyms=AOP1.1; OrderedLocusNames=At4g03070; ORFNames=T4I9.5;
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 [MRNA], AND GENE FAMILY.
RC STRAIN=cv. Columbia;
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).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Probable 2-oxoglutarate-dependent dioxygenase that may be
CC involved in glucosinolates biosynthesis. May play a role in the
CC production of aliphatic glucosinolates (By 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 -!- 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}.
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DR EMBL; AF417855; AAL14643.1; -; mRNA.
DR EMBL; AF069442; AAC79098.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77792.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82267.1; -; Genomic_DNA.
DR PIR; T01386; T01386.
DR RefSeq; NP_192216.1; NM_116541.4.
DR AlphaFoldDB; Q9ZTA3; -.
DR SMR; Q9ZTA3; -.
DR STRING; 3702.AT4G03070.1; -.
DR PaxDb; Q9ZTA3; -.
DR PRIDE; Q9ZTA3; -.
DR ProteomicsDB; 244408; -.
DR EnsemblPlants; AT4G03070.1; AT4G03070.1; AT4G03070.
DR GeneID; 828100; -.
DR Gramene; AT4G03070.1; AT4G03070.1; AT4G03070.
DR KEGG; ath:AT4G03070; -.
DR Araport; AT4G03070; -.
DR TAIR; locus:2139389; AT4G03070.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_3_1_1; -.
DR InParanoid; Q9ZTA3; -.
DR OMA; MHKFSTQ; -.
DR OrthoDB; 830141at2759; -.
DR PhylomeDB; Q9ZTA3; -.
DR PRO; PR:Q9ZTA3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZTA3; baseline and differential.
DR Genevisible; Q9ZTA3; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Oxidoreductase; Reference proteome.
FT CHAIN 1..322
FT /note="Probable 2-oxoglutarate-dependent dioxygenase AOP1"
FT /id="PRO_0000423720"
FT DOMAIN 165..271
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 252
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 262
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 322 AA; 36912 MW; FC1693D8C3418DF6 CRC64;
MDSDFVPPSV SFQLPVIDFS DQNLKPGSSK WDEVTADVLK ALEDYGCFEA SFDKLSVELN
RSVFEAMEDL FELPIPTKQR NVSSKPFHGY LCHNLYESLG INDANVLEKV NDFTQQLWPD
HGNKSISETI HLFSEQLVEL DLMVRRMIME SFGIENYIDE HLNSTYYLTR LMKYTSPPDD
DDDDDEETKL GLRSHTDKNI ITILHQYQVD GLEVKTKDDK WIKVKPSQDS VLVMVGDSLC
ALLNGRLHSP YHRVIMTGKK TRYSTGLFSI PKTGVIIDSP EELVDKEHPR IFKPFEYTDF
LHFFQTEAGR IAQSALHAFA AF
