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GAOX3_ARATH
ID   GAOX3_ARATH             Reviewed;         380 AA.
AC   Q39112;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Gibberellin 20 oxidase 3 {ECO:0000305|PubMed:7630935};
DE            EC=1.14.11.- {ECO:0000269|PubMed:7630935};
DE   AltName: Full=GA 20-oxidase 3;
DE   AltName: Full=Gibberellin C-20 oxidase 3 {ECO:0000305|PubMed:7630935};
GN   Name=GA20OX3; Synonyms=20ox3, YAP169; OrderedLocusNames=At5g07200;
GN   ORFNames=T28J14_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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Silique;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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 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   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION BY 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   [8]
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: Key oxidase enzyme in the biosynthesis of gibberellin that
CC       catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively,
CC       via a three-step oxidation at C-20 of the GA skeleton, and GA25 is also
CC       formed as a minor product. GA53 is less effectively oxidized than GA12.
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=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   -!- 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:0000269|PubMed:7630935};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60797;
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 at high level in developing siliques.
CC       Detected in seeds, roots, leaves and inflorescences. In seeds,
CC       specifically detected at the outer layer of the outer integument.
CC       {ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:18069939,
CC       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. Not regulated by auxin. Up-regulated by paclobutrazol.
CC       {ECO:0000269|PubMed:16905669, 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; X83381; CAA58295.1; -; mRNA.
DR   EMBL; AL163652; CAB87276.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91121.1; -; Genomic_DNA.
DR   EMBL; BT004311; AAO42308.1; -; mRNA.
DR   EMBL; BT005615; AAO64035.1; -; mRNA.
DR   PIR; T48491; T48491.
DR   RefSeq; NP_196337.1; NM_120802.2.
DR   AlphaFoldDB; Q39112; -.
DR   SMR; Q39112; -.
DR   STRING; 3702.AT5G07200.1; -.
DR   iPTMnet; Q39112; -.
DR   PaxDb; Q39112; -.
DR   PRIDE; Q39112; -.
DR   ProteomicsDB; 228964; -.
DR   EnsemblPlants; AT5G07200.1; AT5G07200.1; AT5G07200.
DR   GeneID; 830611; -.
DR   Gramene; AT5G07200.1; AT5G07200.1; AT5G07200.
DR   KEGG; ath:AT5G07200; -.
DR   Araport; AT5G07200; -.
DR   TAIR; locus:2182875; AT5G07200.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_3_1; -.
DR   InParanoid; Q39112; -.
DR   OMA; AYLHMDS; -.
DR   OrthoDB; 755305at2759; -.
DR   PhylomeDB; Q39112; -.
DR   BioCyc; MetaCyc:AT5G07200-MON; -.
DR   UniPathway; UPA00390; -.
DR   PRO; PR:Q39112; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q39112; baseline and differential.
DR   Genevisible; Q39112; AT.
DR   GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0045544; F:gibberellin 20-oxidase activity; IDA:TAIR.
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: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   1: Evidence at protein level;
KW   Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Gibberellin 20 oxidase 3"
FT                   /id="PRO_0000219516"
FT   DOMAIN          221..321
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         248
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         302
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   380 AA;  43437 MW;  0DDEFAB907424056 CRC64;
     MATECIATVP QIFSENKTKE DSSIFDAKLL NQHSHHIPQQ FVWPDHEKPS TDVQPLQVPL
     IDLAGFLSGD SCLASEATRL VSKAATKHGF FLITNHGVDE SLLSRAYLHM DSFFKAPACE
     KQKAQRKWGE SSGYASSFVG RFSSKLPWKE TLSFKFSPEE KIHSQTVKDF VSKKMGDGYE
     DFGKVYQEYA EAMNTLSLKI MELLGMSLGV ERRYFKEFFE DSDSIFRLNY YPQCKQPELA
     LGTGPHCDPT SLTILHQDQV GGLQVFVDNK WQSIPPNPHA FVVNIGDTFM ALTNGRYKSC
     LHRAVVNSER ERKTFAFFLC PKGEKVVKPP EELVNGVKSG ERKYPDFTWS MFLEFTQKHY
     RADMNTLDEF SIWLKNRRSF
 
 
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