G2OX7_ARATH
ID G2OX7_ARATH Reviewed; 336 AA.
AC Q9C6I4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 7;
DE EC=1.14.11.13;
DE AltName: Full=GA 2-oxidase 7;
DE AltName: Full=Gibberellin 2-beta-hydroxylase 7;
DE AltName: Full=Gibberellin 2-oxidase 7;
GN Name=GA2OX7; OrderedLocusNames=At1g50960; ORFNames=F8A12.18;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, AND CHARACTERIZATION.
RX PubMed=12509528; DOI=10.1105/tpc.005975;
RA Schomburg F.M., Bizzell C.M., Lee D.J., Zeevaart J.A.D., Amasino R.M.;
RT "Overexpression of a novel class of gibberellin 2-oxidases decreases
RT gibberellin levels and creates dwarf plants.";
RL Plant Cell 15:151-163(2003).
RN [4]
RP INDUCTION BY AUXIN AND PACLOBUTRAZOL.
RX PubMed=16905669; DOI=10.1104/pp.106.084871;
RA Frigerio M., Alabadi D., Perez-Gomez J., Garcia-Carcel L., Phillips A.L.,
RA Hedden P., Blazquez M.A.;
RT "Transcriptional regulation of gibberellin metabolism genes by auxin
RT signaling in Arabidopsis.";
RL Plant Physiol. 142:553-563(2006).
RN [5]
RP GENE FAMILY.
RX PubMed=21056641; DOI=10.1016/j.gene.2010.10.010;
RA Han F., Zhu B.;
RT "Evolutionary analysis of three gibberellin oxidase genes in rice,
RT Arabidopsis, and soybean.";
RL Gene 473:23-35(2011).
CC -!- FUNCTION: Catalyzes the 2-beta-hydroxylation of gibberellins (GA)
CC precursors, rendering them unable to be converted to active GAs.
CC Hydroxylates the C20-GA GA12 and GA53, but is not active on C19-GAs,
CC like GA1, GA4, GA9 and GA20. {ECO:0000269|PubMed:12509528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A1 + O2 = CO2 + gibberellin A8 +
CC succinate; Xref=Rhea:RHEA:15005, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58524, ChEBI:CHEBI:58594; EC=1.14.11.13;
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 -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- INTERACTION:
CC Q9C6I4; Q9M384: SCR; NbExp=3; IntAct=EBI-25513059, EBI-1250484;
CC -!- INDUCTION: Not regulated by auxin. Down-regulated by paclobutrazol.
CC {ECO:0000269|PubMed:16905669}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
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DR EMBL; AC079284; AAG50945.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32606.1; -; Genomic_DNA.
DR PIR; G96546; G96546.
DR RefSeq; NP_175509.1; NM_103976.2.
DR AlphaFoldDB; Q9C6I4; -.
DR SMR; Q9C6I4; -.
DR BioGRID; 26743; 1.
DR IntAct; Q9C6I4; 1.
DR STRING; 3702.AT1G50960.1; -.
DR PaxDb; Q9C6I4; -.
DR PRIDE; Q9C6I4; -.
DR EnsemblPlants; AT1G50960.1; AT1G50960.1; AT1G50960.
DR GeneID; 841518; -.
DR Gramene; AT1G50960.1; AT1G50960.1; AT1G50960.
DR KEGG; ath:AT1G50960; -.
DR Araport; AT1G50960; -.
DR TAIR; locus:2036386; AT1G50960.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_15_1_1; -.
DR InParanoid; Q9C6I4; -.
DR OMA; AQMICEI; -.
DR OrthoDB; 962097at2759; -.
DR PhylomeDB; Q9C6I4; -.
DR BioCyc; ARA:AT1G50960-MON; -.
DR BioCyc; MetaCyc:AT1G50960-MON; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9C6I4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6I4; baseline and differential.
DR Genevisible; Q9C6I4; AT.
DR GO; GO:0052635; F:C-20 gibberellin 2-beta-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:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009685; P:gibberellin metabolic process; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IGI:TAIR.
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; Oxidoreductase; Reference proteome.
FT CHAIN 1..336
FT /note="Gibberellin 2-beta-dioxygenase 7"
FT /id="PRO_0000067308"
FT DOMAIN 191..291
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 282
FT /evidence="ECO:0000255"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 282
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 336 AA; 38289 MW; BA8A0F6DB4236558 CRC64;
MASQPPFKTN FCSIFGSSFP NSTSESNTNT STIQTSGIKL PVIDLSHLTS GEEVKRKRCV
KQMVAAAKEW GFFQIVNHGI PKDVFEMMLL EEKKLFDQPF SVKVRERFSD LSKNSYRWGN
PSATSPAQYS VSEAFHIILS EVSRISDDRN NLRTIVETYV QEIARVAQMI CEILGKQVNV
SSEYFENIFE LENSFLRLNK YHPSVFGSEV FGLVPHTDTS FLTILSQDQI GGLELENNGQ
WISVKPCLEA LTVNIGDMFQ ALSNGVYQSV RHRVISPANI ERMSIAFFVC PYLETEIDCF
GYPKKYRRFS FREYKEQSEH DVKETGDKVG LSRFLI
