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GAOX2_ARATH
ID   GAOX2_ARATH             Reviewed;         378 AA.
AC   Q39111;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Gibberellin 20 oxidase 2 {ECO:0000305|PubMed:7630935};
DE            EC=1.14.11.- {ECO:0000269|PubMed:7630935};
DE   AltName: Full=GA 20-oxidase 2 {ECO:0000305|PubMed:7630935};
DE   AltName: Full=Gibberellin C-20 oxidase 2;
GN   Name=GA20OX2; Synonyms=20ox, At2353; OrderedLocusNames=At5g51810;
GN   ORFNames=MIO24.5;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Flower bud, and Stem;
RX   PubMed=7630935; DOI=10.1104/pp.108.3.1049;
RA   Phillips A.L., Ward D.A., Uknes S., Appleford N.E.J., Lange T.,
RA   Huttly A.K., Gaskin P., Graebe J.E., Hedden P.;
RT   "Isolation and expression of three gibberellin 20-oxidase cDNA clones from
RT   Arabidopsis.";
RL   Plant Physiol. 108:1049-1057(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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).
RN   [4]
RP   INDUCTION BY COLD.
RX   PubMed=14729916; DOI=10.1105/tpc.018143;
RA   Yamauchi Y., Ogawa M., Kuwahara A., Hanada A., Kamiya Y., Yamaguchi S.;
RT   "Activation of gibberellin biosynthesis and response pathways by low
RT   temperature during imbibition of Arabidopsis thaliana seeds.";
RL   Plant Cell 16:367-378(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=15927942; DOI=10.1093/pcp/pci141;
RA   Kim Y.C., Nakajima M., Nakayama A., Yamaguchi I.;
RT   "Contribution of gibberellins to the formation of Arabidopsis seed coat
RT   through starch degradation.";
RL   Plant Cell Physiol. 46:1317-1325(2005).
RN   [6]
RP   INDUCTION BY LIGHT.
RX   PubMed=15923331; DOI=10.1104/pp.104.059055;
RA   Hisamatsu T., King R.W., Helliwell C.A., Koshioka M.;
RT   "The involvement of gibberellin 20-oxidase genes in phytochrome-regulated
RT   petiole elongation of Arabidopsis.";
RL   Plant Physiol. 138:1106-1116(2005).
RN   [7]
RP   INDUCTION BY AUXIN AND PACLOBUTRAZOL, AND TISSUE SPECIFICITY.
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   [8]
RP   FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP   GIBBERELLIN.
RC   STRAIN=cv. Columbia;
RX   PubMed=18069939; DOI=10.1111/j.1365-313x.2007.03356.x;
RA   Rieu I., Ruiz-Rivero O., Fernandez-Garcia N., Griffiths J., Powers S.J.,
RA   Gong F., Linhartova T., Eriksson S., Nilsson O., Thomas S.G.,
RA   Phillips A.L., Hedden P.;
RT   "The gibberellin biosynthetic genes AtGA20ox1 and AtGA20ox2 act, partially
RT   redundantly, to promote growth and development throughout the Arabidopsis
RT   life cycle.";
RL   Plant J. 53:488-504(2008).
RN   [9]
RP   3D-STRUCTURE MODELING, AND 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: Key oxidase enzyme in the biosynthesis of gibberellin that
CC       catalyzes the conversion of GA12 to GA9, via a three-step oxidation at
CC       C-20 of the GA skeleton, and GA25 is also formed as a minor product.
CC       GA53 is less effectively oxidized than GA12 and is only oxidized one
CC       step to GA44 (PubMed:7630935). Involved in the promotion of the floral
CC       transition, fertility and silique elongation, but plays only a minor
CC       role in elongation of seedling organs. Acts redundantly with GA20OX1
CC       (PubMed:18069939). {ECO:0000269|PubMed:18069939,
CC       ECO:0000269|PubMed:7630935}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + gibberellin A12 + H(+) + 3 O2 = 3 CO2 +
CC         gibberellin A9 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60772,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58627, ChEBI:CHEBI:73255;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + gibberellin A12 + O2 = CO2 + gibberellin A15
CC         + succinate; Xref=Rhea:RHEA:60776, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58627, ChEBI:CHEBI:143956;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60777;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + gibberellin A15 + O2 = CO2 + gibberellin A24
CC         + H2O + succinate; Xref=Rhea:RHEA:60780, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:143956, ChEBI:CHEBI:143957;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60781;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + gibberellin A53 + O2 = CO2 + gibberellin A44
CC         + succinate; Xref=Rhea:RHEA:60800, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:143954, ChEBI:CHEBI:143955;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60801;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 2-oxoglutarate + gibberellin A12 + 3 O2 = 3 CO2 +
CC         gibberellin A25 + H(+) + H2O + 3 succinate; Xref=Rhea:RHEA:60768,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58627, ChEBI:CHEBI:143959;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60769;
CC         Evidence={ECO:0000269|PubMed:7630935};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Fe(2+) ion per subunit.;
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Expressed in inflorescence and developing siliques.
CC       Detected in seeds, roots, cotyledons and leaves. In seeds, specifically
CC       detected at the rim of the embryo and the outer integument.
CC       {ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:16905669,
CC       ECO:0000269|PubMed:18069939, ECO:0000269|PubMed:7630935}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing siliques 3-13 days after
CC       pollination. {ECO:0000269|PubMed:15927942}.
CC   -!- INDUCTION: Negatively controlled by the level of physiologically active
CC       gibberellin. Up-regulated by auxin, paclobutrazol, long day exposure
CC       and cold treatment. {ECO:0000269|PubMed:14729916,
CC       ECO:0000269|PubMed:15923331, ECO:0000269|PubMed:16905669,
CC       ECO:0000269|PubMed:18069939}.
CC   -!- DISRUPTION PHENOTYPE: Slightly smaller than the wild type.
CC       {ECO:0000269|PubMed:18069939}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA20OX subfamily. {ECO:0000305}.
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DR   EMBL; X83380; CAA58294.1; -; mRNA.
DR   EMBL; AB010074; BAB11250.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96129.1; -; Genomic_DNA.
DR   RefSeq; NP_199994.1; NM_124560.4.
DR   AlphaFoldDB; Q39111; -.
DR   SMR; Q39111; -.
DR   STRING; 3702.AT5G51810.1; -.
DR   PaxDb; Q39111; -.
DR   PRIDE; Q39111; -.
DR   ProteomicsDB; 228896; -.
DR   EnsemblPlants; AT5G51810.1; AT5G51810.1; AT5G51810.
DR   GeneID; 835256; -.
DR   Gramene; AT5G51810.1; AT5G51810.1; AT5G51810.
DR   KEGG; ath:AT5G51810; -.
DR   Araport; AT5G51810; -.
DR   TAIR; locus:2165341; AT5G51810.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_3_1; -.
DR   InParanoid; Q39111; -.
DR   OMA; NVRAVHY; -.
DR   OrthoDB; 755305at2759; -.
DR   PhylomeDB; Q39111; -.
DR   BioCyc; ARA:AT5G51810-MON; -.
DR   BioCyc; MetaCyc:AT5G51810-MON; -.
DR   BRENDA; 1.14.11.12; 399.
DR   UniPathway; UPA00390; -.
DR   PRO; PR:Q39111; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q39111; baseline and differential.
DR   Genevisible; Q39111; AT.
DR   GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0103055; F:gibberelli A15, 2-oxoglutarate:oxygen oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0045544; F:gibberellin 20-oxidase activity; IDA:TAIR.
DR   GO; GO:0103054; F:gibberellin A12, 2-oxoglutarate:oxygen oxidoreductase activity (gibberellin A15-forming); IEA:RHEA.
DR   GO; GO:0103056; F:gibberellin A53, 2-oxoglutarate:oxygen oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009908; P:flower development; IBA:GO_Central.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IDA:TAIR.
DR   GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR   GO; GO:0009639; P:response to red or far red light; IEP:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IBA:GO_Central.
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   Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Gibberellin 20 oxidase 2"
FT                   /id="PRO_0000219515"
FT   DOMAIN          220..320
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000255"
FT   BINDING         245
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         247
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   378 AA;  42937 MW;  0B5CF4E6FDBD2B74 CRC64;
     MAILCTTTSP AEKEHEPKQD LEKDQTSPLI FNPSLLNLQS QIPNQFIWPD EEKPSIDIPE
     LNVPFIDLSS QDSTLEAPRV IAEACTKHGF FLVVNHGVSE SLIADAHRLM ESFFDMPLAG
     KQKAQRKPGE SCGYASSFTG RFSTKLPWKE TLSFQFSNDN SGSRTVQDYF SDTLGQEFEQ
     FGKVYQDYCE AMSSLSLKIM ELLGLSLGVN RDYFRGFFEE NDSIMRLNHY PPCQTPDLTL
     GTGPHCDPSS LTILHQDHVN GLQVFVDNQW QSIRPNPKAF VVNIGDTFMA LSNGIFKSCL
     HRAVVNRESA RKSMAFFLCP KKDKVVKPPS DILEKMKTRK YPDFTWSMFL EFTQKHYRAD
     VNTLDSFSNW VITNNNPI
 
 
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