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G2OX8_ARATH
ID   G2OX8_ARATH             Reviewed;         338 AA.
AC   O49561; A0MF87; Q1PE62;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Gibberellin 2-beta-dioxygenase 8;
DE            EC=1.14.11.13;
DE   AltName: Full=GA 2-oxidase 8;
DE   AltName: Full=Gibberellin 2-beta-hydroxylase 8;
DE   AltName: Full=Gibberellin 2-oxidase 8;
GN   Name=GA2OX8; OrderedLocusNames=At4g21200; ORFNames=F7J7.140;
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
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   [5]
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   [6]
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   -!- 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=O49561-1; Sequence=Displayed;
CC   -!- INDUCTION: Up-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28642.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA17539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL021960; CAA17539.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161554; CAB79120.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84420.1; -; Genomic_DNA.
DR   EMBL; DQ446856; ABE66080.1; -; mRNA.
DR   EMBL; DQ653213; ABK28642.1; ALT_SEQ; mRNA.
DR   PIR; T04951; T04951.
DR   RefSeq; NP_193852.2; NM_118239.3. [O49561-1]
DR   AlphaFoldDB; O49561; -.
DR   SMR; O49561; -.
DR   STRING; 3702.AT4G21200.1; -.
DR   PaxDb; O49561; -.
DR   PRIDE; O49561; -.
DR   EnsemblPlants; AT4G21200.1; AT4G21200.1; AT4G21200. [O49561-1]
DR   GeneID; 827868; -.
DR   Gramene; AT4G21200.1; AT4G21200.1; AT4G21200. [O49561-1]
DR   KEGG; ath:AT4G21200; -.
DR   Araport; AT4G21200; -.
DR   TAIR; locus:2127403; AT4G21200.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_15_1_1; -.
DR   InParanoid; O49561; -.
DR   OMA; KPFHEKM; -.
DR   OrthoDB; 622449at2759; -.
DR   PhylomeDB; O49561; -.
DR   BRENDA; 1.14.11.13; 399.
DR   UniPathway; UPA00390; -.
DR   PRO; PR:O49561; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49561; baseline and differential.
DR   Genevisible; O49561; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
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:0010336; P:gibberellic acid homeostasis; IEA:EnsemblPlants.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045487; P:gibberellin catabolic process; IEA:EnsemblPlants.
DR   GO; GO:0009685; P:gibberellin metabolic process; IDA: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   Alternative splicing; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..338
FT                   /note="Gibberellin 2-beta-dioxygenase 8"
FT                   /id="PRO_0000067309"
FT   DOMAIN          191..290
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000255"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         217
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         271
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         281
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   338 AA;  39086 MW;  8E2536F78FC3786F CRC64;
     MDPPFNEIYN NLLYNQITKK DNDVSEIPFS FSVTAVVEEV ELPVIDVSRL IDGAEEEREK
     CKEAIARASR EWGFFQVINH GISMDVLEKM RQEQIRVFRE PFDKKSKSEK FSAGSYRWGT
     PSATSIRQLS WSEAFHVPMT DISDNKDFTT LSSTMEKFAS ESEALAYMLA EVLAEKSGQN
     SSFFKENCVR NTCYLRMNRY PPCPKPSEVY GLMPHTDSDF LTILYQDQVG GLQLIKDNRW
     IAVKPNPKAL IINIGDLFQA WSNGMYKSVE HRVMTNPKVE RFSTAYFMCP SYDAVIECSS
     DRPAYRNFSF REFRQQVQED VKKFGFKVGL PRFLNHVY
 
 
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