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GAOX1_ORYSJ
ID   GAOX1_ORYSJ             Reviewed;         372 AA.
AC   P93771; Q10AC7; Q84M83;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Gibberellin 20 oxidase 1 {ECO:0000303|PubMed:12834406};
DE            Short=OsGA20ox1 {ECO:0000303|PubMed:12834406};
DE            EC=1.14.11.- {ECO:0000305};
DE   AltName: Full=GA 20-oxidase 1 {ECO:0000303|PubMed:12834406};
DE   AltName: Full=Gibberellin C-20 oxidase 1 {ECO:0000305};
DE   AltName: Full=Os20ox {ECO:0000303|Ref.1};
GN   Name=GA20OX1 {ECO:0000305};
GN   Synonyms=20ox1 {ECO:0000305}, GA20ox-1 {ECO:0000305};
GN   OrderedLocusNames=Os03g0856700 {ECO:0000312|EMBL:BAF13865.1},
GN   LOC_Os03g63970 {ECO:0000312|EMBL:ABF99990.1};
GN   ORFNames=OSJNBa0059G06.22 {ECO:0000312|EMBL:AAP21386.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC   STRAIN=cv. Nipponbare;
RX   DOI=10.1111/j.1399-3054.1997.tb03438.x;
RA   Toyomasu T., Kawaide H., Sekimoto H., von Numers C., Phillips A.L.,
RA   Hedden P., Kamiya Y.;
RT   "Cloning and characterization of a cDNA encoding gibberellin 20-oxidase
RT   from rice (Oryza sativa) seedlings.";
RL   Physiol. Plantarum 99:111-118(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=11961544; DOI=10.1038/416701a;
RA   Sasaki A., Ashikari M., Ueguchi-Tanaka M., Itoh H., Nishimura A.,
RA   Swapan D., Ishiyama K., Saito T., Kobayashi M., Khush G.S., Kitano H.,
RA   Matsuoka M.;
RT   "A mutant gibberellin-synthesis gene in rice.";
RL   Nature 416:701-702(2002).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=12834406; DOI=10.1046/j.1365-313x.2003.01780.x;
RA   Kaneko M., Itoh H., Inukai Y., Sakamoto T., Ueguchi-Tanaka M., Ashikari M.,
RA   Matsuoka M.;
RT   "Where do gibberellin biosynthesis and gibberellin signaling occur in rice
RT   plants?";
RL   Plant J. 35:104-115(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=15604710; DOI=10.1007/s11103-004-1692-y;
RA   Oikawa T., Koshioka M., Kojima K., Yoshida H., Kawata M.;
RT   "A role of OsGA20ox1, encoding an isoform of gibberellin 20-oxidase, for
RT   regulation of plant stature in rice.";
RL   Plant Mol. Biol. 55:687-700(2004).
CC   -!- FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin (Ref.1,
CC       PubMed:15604710). Catalyzes the conversion of GA12 and GA53 to GA9 and
CC       GA20 respectively, via a three-step oxidation at C-20 of the GA
CC       skeleton (Ref.1). {ECO:0000269|PubMed:15604710, ECO:0000269|Ref.1}.
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:0000250|UniProtKB:O04705};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC         Evidence={ECO:0000250|UniProtKB:O04705};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + gibberellin A53 + H(+) + 3 O2 = 3 CO2 +
CC         gibberellin A20 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60796,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58526, ChEBI:CHEBI:143954;
CC         Evidence={ECO:0000250|UniProtKB:O04705};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60797;
CC         Evidence={ECO:0000250|UniProtKB:O04705};
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   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in reproductive organs
CC       (PubMed:11961544). Expressed in the epithelium of embryos and the
CC       tapetum of anthers. Expressed at low levels in the shoot apical
CC       meristem (PubMed:12834406). {ECO:0000269|PubMed:11961544,
CC       ECO:0000269|PubMed:12834406}.
CC   -!- INDUCTION: Negatively controlled by the level of physiologically active
CC       gibberellin. {ECO:0000269|Ref.1}.
CC   -!- MISCELLANEOUS: Plants over-expressing GA20OX1 have high levels of
CC       bioactive gibberellins, and exhibit an overgrowth phenotype with
CC       increased internode elongation and leaf sheath length
CC       (PubMed:15604710). Plant silencing GA20OX1 exhibit a semi-dwarf
CC       phenotype (PubMed:15604710). {ECO:0000269|PubMed:15604710}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA20OX subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP21386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U50333; AAB48239.1; -; mRNA.
DR   EMBL; AC096690; AAP21386.1; ALT_INIT; Genomic_DNA.
DR   EMBL; DP000009; ABF99990.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13865.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS87451.1; -; Genomic_DNA.
DR   EMBL; AK099111; BAG93931.1; -; mRNA.
DR   PIR; T04337; T04337.
DR   RefSeq; XP_015628526.1; XM_015773040.1.
DR   AlphaFoldDB; P93771; -.
DR   SMR; P93771; -.
DR   STRING; 4530.OS03T0856700-01; -.
DR   PaxDb; P93771; -.
DR   PRIDE; P93771; -.
DR   EnsemblPlants; Os03t0856700-01; Os03t0856700-01; Os03g0856700.
DR   EnsemblPlants; Os03t0856700-02; Os03t0856700-02; Os03g0856700.
DR   GeneID; 4334841; -.
DR   Gramene; Os03t0856700-01; Os03t0856700-01; Os03g0856700.
DR   Gramene; Os03t0856700-02; Os03t0856700-02; Os03g0856700.
DR   KEGG; osa:4334841; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_3_1; -.
DR   InParanoid; P93771; -.
DR   OMA; NVRAVHY; -.
DR   OrthoDB; 755305at2759; -.
DR   BRENDA; 1.14.11.13; 4460.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; P93771; OS.
DR   GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0045544; F:gibberellin 20-oxidase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0009685; P:gibberellin metabolic process; IC:Gramene.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..372
FT                   /note="Gibberellin 20 oxidase 1"
FT                   /id="PRO_0000219517"
FT   DOMAIN          209..309
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255"
FT   BINDING         234
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         236
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         290
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   CONFLICT        107..116
FT                   /note="AQRRAGESCG -> RSGARGRTA (in Ref. 1; AAB48239)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352..353
FT                   /note="TL -> LF (in Ref. 1; AAB48239)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  42256 MW;  6BC532897F731C27 CRC64;
     MSMVVQQEQE VVFDAAVLSG QTEIPSQFIW PAEESPGSVA VEELEVALID VGAGAERSSV
     VRQVGEACER HGFFLVVNHG IEAALLEEAH RCMDAFFTLP LGEKQRAQRR AGESCGYASS
     FTGRFASKLP WKETLSFRYS SAGDEEGEEG VGEYLVRKLG AEHGRRLGEV YSRYCHEMSR
     LSLELMEVLG ESLGIVGDRR HYFRRFFQRN DSIMRLNYYP ACQRPLDTLG TGPHCDPTSL
     TILHQDHVGG LEVWAEGRWR AIRPRPGALV VNVGDTFMAL SNARYRSCLH RAVVNSTAPR
     RSLAFFLCPE MDTVVRPPEE LVDDHHPRVY PDFTWRALLD FTQRHYRADM RTLQAFSDWL
     NHHRHLQPTI YS
 
 
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