ID A0A3L6SUJ4_PANMI Unreviewed; 367 AA.
AC A0A3L6SUJ4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Gibberellin 2-beta-dioxygenase 6-like {ECO:0000313|EMBL:RLN28160.1};
GN ORFNames=C2845_PM05G12720 {ECO:0000313|EMBL:RLN28160.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN28160.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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. {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:RLN28160.1}.
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DR EMBL; PQIB02000003; RLN28160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6SUJ4; -.
DR STRING; 4540.A0A3L6SUJ4; -.
DR Proteomes; UP000275267; Chromosome 5.
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:SF251; GIBBERELLIN 2-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:RLN28160.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267}.
FT DOMAIN 173..305
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 39205 MW; 460AD16B4C98C117 CRC64;
MVVPSTTPVR QGTAASHGGG IPTVDMSAPG GRGALSRQVA RACAEHGFFR AVSHGVPPGP
AARLDAATAA FFALAPHDKQ RAGPPSPLGY GCRSIGFNGD AGELEYLLLH ASPAAVAHRA
RSIDTDDPSR FSTVVNDYVG AVRQLACEIL DLLGEGLGLK DPGSFSKLIT DTDSDSLLRI
NHYPPACTIH KLDHDDQCKM KSIVRTKNGN GLNPSAGARI GFGEHSDPQI ISLLRANDVN
GLQVLLPNSD GKEVWVQVPA DPSAFFVNVG DLLQALTNGK LVSVRHRVIA SACRPRLSTI
YFAAPPLHAR ISALPETITA DSPCRYRPFT WTEYKKTMYS LRLSHSRLDL FQVGDDDSSN
VGKGEQE
//
