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Database: UniProt
Entry: G7IC45_MEDTR
LinkDB: G7IC45_MEDTR
Original site: G7IC45_MEDTR 
ID   G7IC45_MEDTR            Unreviewed;       377 AA.
AC   G7IC45; A0A0C3UU26;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 2.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Gibberellin 20-oxidase {ECO:0000313|EMBL:AES62614.2};
DE   SubName: Full=Putative gibberellin-44 dioxygenase {ECO:0000313|EMBL:RHN81911.1};
DE            EC=1.14.11.12 {ECO:0000313|EMBL:RHN81911.1};
GN   Name=11415102 {ECO:0000313|EnsemblPlants:AES62614};
GN   OrderedLocusNames=MTR_1g102070 {ECO:0000313|EMBL:AES62614.2};
GN   ORFNames=MtrunA17_Chr1g0204181 {ECO:0000313|EMBL:RHN81911.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES62614.2, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES62614.2, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES62614.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES62614,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES62614.2, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES62614,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES62614}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES62614};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|Proteomes:UP000265566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX   PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA   Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA   Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA   Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA   Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA   Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA   Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 4:1017-1025(2018).
RN   [5] {ECO:0000313|EMBL:RHN81911.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN81911.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
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:0000256|ARBA:ARBA00043814};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC         Evidence={ECO:0000256|ARBA:ARBA00043814};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA20OX subfamily. {ECO:0000256|ARBA:ARBA00043997}.
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DR   EMBL; CM001217; AES62614.2; -; Genomic_DNA.
DR   EMBL; PSQE01000001; RHN81911.1; -; Genomic_DNA.
DR   RefSeq; XP_003592363.2; XM_003592315.2.
DR   AlphaFoldDB; G7IC45; -.
DR   STRING; 3880.G7IC45; -.
DR   PaxDb; 3880-AES62614; -.
DR   EnsemblPlants; AES62614; AES62614; MTR_1g102070.
DR   GeneID; 11415102; -.
DR   Gramene; AES62614; AES62614; MTR_1g102070.
DR   KEGG; mtr:11415102; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_3_1; -.
DR   OrthoDB; 1057251at2759; -.
DR   Proteomes; UP000002051; Chromosome 1.
DR   Proteomes; UP000265566; Chromosome 1.
DR   ExpressionAtlas; G7IC45; differential.
DR   GO; GO:0045544; F:gibberellin 20-oxidase activity; IBA:GO_Central.
DR   GO; GO:0047927; F:gibberellin-44 dioxygenase activity; IEA:UniProtKB-EC.
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   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   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF53; GIBBERELLIN 20 OXIDASE 1; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:RHN81911.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682,
KW   ECO:0000313|EMBL:RHN81911.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN          222..321
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   377 AA;  42777 MW;  CFFC7FC8C4211181 CRC64;
     MAIECITSMP QQLLNQETKE QEKPLVFDAS VLKHQVNLPT QFIWPDEEQA CLNVPELHVP
     FIDLGGFLSG DPVAAMEASK VVGEACKKHG FFLVVNHGID EKLISDAHAF MDDFFELPLS
     QKQRAQRKTG EHCGYASSFT GRFSSKLPWK ETLSFQFSAD EKSPNLVRDY LCNTMGNEFE
     KFGEVYQDYC KAMSNLSLGI MEILGMSLGV GKAHFREFFE ENSSIMRLNY YPTCQKPELT
     LGTGPHCDPT SLTILHQDQV GGLQVYVDDQ WHSISPHFNA FVVNIGDTFM ALSNGRYKSC
     LHRAVVNSEK TRKSLAFFLC PLSDKVVTPP CELVDNYNPR IYPDFTWSML LEFTQKHYRA
     DIKTLEAFAK WVQCKST
//
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