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Database: UniProt
Entry: A0A067FA78_CITSI
LinkDB: A0A067FA78_CITSI
Original site: A0A067FA78_CITSI 
ID   A0A067FA78_CITSI        Unreviewed;       361 AA.
AC   A0A067FA78;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=feruloyl-CoA 6-hydroxylase {ECO:0000256|ARBA:ARBA00012885};
DE            EC=1.14.11.61 {ECO:0000256|ARBA:ARBA00012885};
GN   ORFNames=CISIN_1g018077mg {ECO:0000313|EMBL:KDO63055.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO63055.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO63055.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KK784915; KDO63055.1; -; Genomic_DNA.
DR   RefSeq; XP_006488907.1; XM_006488844.2.
DR   AlphaFoldDB; A0A067FA78; -.
DR   SMR; A0A067FA78; -.
DR   STRING; 2711.A0A067FA78; -.
DR   PaxDb; 2711-XP_006488907-1; -.
DR   GeneID; 102613413; -.
DR   KEGG; cit:102613413; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   OrthoDB; 1211890at2759; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProt.
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   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:UP000027120}.
FT   DOMAIN          208..309
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   361 AA;  40272 MW;  7D9782F1AFB0D95A CRC64;
     MAPTTVLLSD FSDVTDFVVN QGNGVKGLSE MGLKALPKQY IQPLEERFSE KKIVPHESIP
     IIDMSKWDDP EVAKSICDAA EMWGFFQVVN HRVPLQVLDR VKAATHRFFG LSAAEKNKYS
     KELSPSNNVR FGTSFNTQAE KALEWKDYLS LFYVSDDEAS ALWPPACKDE VLEYTKSSEV
     LIKQLLKVLM KGLKVEGTDE AKEALLMGSV RTNLNYYPIC PNPELTVGVG RHSDVSTLTI
     LLQDDIGGLY VRGNDGESWI HVPPISGSLV INIGDALQIM SNGKYRSVEH CVIANGSSNR
     ISVPIFINPR PQDTIGPFPE VLASGEKPVY KQVLYKDYVK HFFRKAHDGK KTVDFAKLSI
     F
//
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