ID A0A443N419_9MAGN Unreviewed; 354 AA.
AC A0A443N419;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Gibberellin 3-beta-dioxygenase 1-like protein {ECO:0000313|EMBL:RWR73252.1};
GN ORFNames=CKAN_00151300 {ECO:0000313|EMBL:RWR73252.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR73252.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR73252.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR73252.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR73252.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QPKB01000001; RWR73252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443N419; -.
DR STRING; 337451.A0A443N419; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF105; GIBBERELLIN 3-BETA-DIOXYGENASE 1; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:RWR73252.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530}.
FT DOMAIN 198..303
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 354 AA; 39612 MW; DA9C59D60087895F CRC64;
MPSLSEAFRA HPVHLHHSHL DFGSVKEVPD THAWPPLDEH LSGDKFDVES VPVIDLGDPN
VVSHIGHACE TWGVFHITNH GISKQLLSDV ESQGRHLFSL PTQQKLKAAR HPDGVAGYGL
VRISSFFSKL MWSEGFTIVG SPLEHARQLW PCDYIQFCNV MEEYEKEMKK LSGRLMLLIL
ESLGLKKEDV KWAGPAGKFE DTCAAIQLNW YPACPDPTRA MGLAEHTDSP LITILHQSST
SGLQVFRERG QRWITVAPLS GSLVVNVGDL LHILSNARFH SVLHRAVVNR TQQRLSVAYL
WGPPAHIEIS PSPQLLTPDR PRLYRAVSLA EYLIIKAKHF NNALAFIRLN PLVN
//