ID A0A1R3JQD2_9ROSI Unreviewed; 299 AA.
AC A0A1R3JQD2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=feruloyl-CoA 6-hydroxylase {ECO:0000256|ARBA:ARBA00012885};
DE EC=1.14.11.61 {ECO:0000256|ARBA:ARBA00012885};
GN ORFNames=COLO4_14993 {ECO:0000313|EMBL:OMO96917.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO96917.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-
CC hydroxyferuloyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57856,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:87305, ChEBI:CHEBI:142390;
CC EC=1.14.11.61; Evidence={ECO:0000256|ARBA:ARBA00000471};
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:OMO96917.1}.
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DR EMBL; AWUE01015536; OMO96917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JQD2; -.
DR STRING; 93759.A0A1R3JQD2; -.
DR OrthoDB; 1057251at2759; -.
DR Proteomes; UP000187203; 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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; PTHR10209:SF243; FERULOYL COA ORTHO-HYDROXYLASE 1-RELATED; 1.
DR PANTHER; PTHR10209; OXIDOREDUCTASE, 2OG-FE II OXYGENASE FAMILY PROTEIN; 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:OMO96917.1};
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:UP000187203}.
FT DOMAIN 141..250
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 299 AA; 33301 MW; 52654C7CA3EF7BC8 CRC64;
MAPTLAEPFA DSSALTEFVI NQGNGVKGLS ELGLRALPKQ YIQPLEERLC MTNVVQQESI
PIIDMSNWED PQVAKSICDA ASKWGFFQIV NHDVPVQVLE NVKEATYRDQ VLDYMKKSEV
VIKQLLQVLM KGLNVTEIDQ TKESLLMGSM RTNLNYYPIC PNPELTVGVG RHSDVSTLTI
LLQDEIGGLY VRADKGDKNW IHVPPIKGSL VINVGDALQI LSNGRYRSVE HRVVANGSKN
RISVPIFVNP KPGDMIGPLP ELVASGEKPI YKQVLYSDYV KHFFRKAHDG KQTVAFAEL
//
