DV4H_CATRO
ID DV4H_CATRO Reviewed; 401 AA.
AC O04847;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Deacetoxyvindoline 4-hydroxylase {ECO:0000303|PubMed:9290645};
DE EC=1.14.11.20 {ECO:0000269|PubMed:8449913, ECO:0000269|PubMed:9290645};
GN Name=D4H {ECO:0000303|PubMed:9290645};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 28-44;
RP 120-137 AND 361-373, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Little Delicata; TISSUE=Seedling;
RX PubMed=9290645; DOI=10.1023/a:1005894001516;
RA Vazquez-Flota F., De Carolis E., Alarco A.-M., De Luca V.;
RT "Molecular cloning and characterization of desacetoxyvindoline-4-
RT hydroxylase, a 2-oxoglutarate dependent-dioxygenase involved in the
RT biosynthesis of vindoline in Catharanthus roseus (L.) G. Don.";
RL Plant Mol. Biol. 34:935-948(1997).
RN [2]
RP CATALYTIC ACTIVITY, CHARACTERIZATION, COFACTOR, AND SUBUNIT.
RC TISSUE=Apical bud, and Leaf;
RX PubMed=8449913; DOI=10.1016/s0021-9258(18)53349-4;
RA De Carolis E., De Luca V.;
RT "Purification, characterization, and kinetic analysis of a 2-oxoglutarate-
RT dependent dioxygenase involved in vindoline biosynthesis from Catharanthus
RT roseus.";
RL J. Biol. Chem. 268:5504-5511(1993).
RN [3]
RP CHARACTERIZATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Leaf, and Shoot apex;
RX PubMed=16667836; DOI=10.1104/pp.94.3.1323;
RA De Carolis E., Chan F., Balsevich J., De Luca V.;
RT "Isolation and characterization of a 2-oxoglutarate dependent dioxygenase
RT involved in the second-to-last step in vindoline biosynthesis.";
RL Plant Physiol. 94:1323-1329(1990).
RN [4]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=21047699; DOI=10.1016/j.jplph.2010.08.018;
RA Guirimand G., Guihur A., Poutrain P., Hericourt F., Mahroug S.,
RA St-Pierre B., Burlat V., Courdavault V.;
RT "Spatial organization of the vindoline biosynthetic pathway in Catharanthus
RT roseus.";
RL J. Plant Physiol. 168:549-557(2011).
CC -!- FUNCTION: Catalyzes the C4-hydroxylation of desacetoxyvindoline.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + deacetoxyvindoline + O2 = 4-O-
CC deacetylvindoline + CO2 + succinate; Xref=Rhea:RHEA:18973,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57965, ChEBI:CHEBI:58461;
CC EC=1.14.11.20; Evidence={ECO:0000269|PubMed:8449913,
CC ECO:0000269|PubMed:9290645};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:8449913};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC -!- PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21047699,
CC ECO:0000305|PubMed:8449913}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21047699}. Nucleus
CC {ECO:0000269|PubMed:21047699}.
CC -!- TISSUE SPECIFICITY: Highest levels in leaves, lower levels in stems and
CC fruits. Not expressed in flowers and roots.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:16667836}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF008597; AAB97311.1; -; Genomic_DNA.
DR EMBL; U71604; AAC49826.1; -; mRNA.
DR EMBL; U71605; AAC49827.1; -; mRNA.
DR PIR; T07914; T07914.
DR AlphaFoldDB; O04847; -.
DR SMR; O04847; -.
DR KEGG; ag:AAB97311; -.
DR BRENDA; 1.14.11.20; 1211.
DR UniPathway; UPA00365; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0050590; F:desacetoxyvindoline 4-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
DR Gene3D; 2.60.120.330; -; 1.
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 Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Cytoplasm; Dioxygenase; Direct protein sequencing;
KW Iron; Metal-binding; Nucleus; Oxidoreductase; Vitamin C.
FT CHAIN 1..401
FT /note="Deacetoxyvindoline 4-hydroxylase"
FT /id="PRO_0000067282"
FT DOMAIN 242..345
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 324
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 334
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 136
FT /note="D -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 45647 MW; 95B66916E01C8979 CRC64;
MPKSWPIVIS SHSFCFLPNS EQERKMKDLN FHAATLSEEE SLRELKAFDE TKAGVKGIVD
TGITKIPRIF IDQPKNLDRI SVCRGKSDIK IPVINLNGLS SNSEIRREIV EKIGEASEKY
GFFQIVNHGI PQDVMDKMVD GVRKFHEQDD QIKRQYYSRD RFNKNFLYSS NYVLIPGIAC
NWRDTMECIM NSNQPDPQEF PDVCRDILMK YSNYVRNLGL ILFELLSEAL GLKPNHLEEM
DCAEGLILLG HYYPACPQPE LTFGTSKHSD SGFLTILMQD QIGGLQILLE NQWIDVPFIP
GALVINIADL LQLITNDKFK SVEHRVLANK VGPRISVAVA FGIKTQTQEG VSPRLYGPIK
ELISEENPPI YKEVTVKDFI TIRFAKRFDD SSSLSPFRLN N
