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Q96323 (LDOX_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucoanthocyanidin dioxygenase

Short name=LDOX
Short name=Leucocyanidin oxygenase
EC=1.14.11.19
Alternative name(s):
Anthocyanidin synthase
Short name=ANS
Leucoanthocyanidin hydroxylase
Protein TANNIN DEFICIENT SEED 4
Short name=TDS4
Protein TRANSPARENT TESTA 11
Short name=TT11
Protein TRANSPARENT TESTA 17
Short name=TT17
Protein TRANSPARENT TESTA 18
Short name=TT18
Gene names
Name:LDOX
Ordered Locus Names:At4g22880
ORF Names:F7H19.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in anthocyanin and protoanthocyanidin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins. Possesses low flavonol synthase activity in vitro towards dihydrokaempferol and dihydroquercetin producing kaempferol and quercitin, respectively. Ref.6 Ref.7 Ref.9 Ref.11 Ref.14

Catalytic activity

Leucocyanidin + 2-oxoglutarate + O2 = cis- and trans-dihydroquercetins + succinate + CO2 + H2O. Ref.7

Cofactor

Binds 1 ascorbate molecule per subunit.

Binds 1 Fe2+ ion per subunit.

Pathway

Pigment biosynthesis; anthocyanin biosynthesis.

Tissue specificity

Expressed in young seedlings (at protein level). Ref.5

Induction

By methyl jasmonate, 6-benzylaminopurine, light and sucrose. Ref.1 Ref.8 Ref.10

Disruption phenotype

No accumulation of anthocyanins, accumulation of protoanthocyanidin intermediates and presence of numerous small vacuoles in leaf epidermal cells. Ref.6 Ref.9 Ref.11

Sequence similarities

Belongs to the iron/ascorbate-dependent oxidoreductase family.

Contains 1 Fe2OG dioxygenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Leucoanthocyanidin dioxygenase
PRO_0000067299

Regions

Domain208 – 307100Fe2OG dioxygenase
Region215 – 21732-oxoglutarate binding
Region298 – 30032-oxoglutarate binding

Sites

Metal binding2321Iron; catalytic
Metal binding2341Iron; catalytic
Metal binding2881Iron; catalytic
Binding site1421Substrate
Binding site2131Substrate
Binding site2331Substrate
Binding site3061Substrate
Binding site3411Substrate

Experimental info

Mutagenesis781G → E in tt11-2; no accumulation of anthocyanin. Ref.11
Mutagenesis1281K → A: Retains two-third of the original activity. Ref.14
Mutagenesis1311N → A or D: Retains two-third of the original activity. Ref.14
Mutagenesis1421Y → H: Retains two-third of the original activity. Ref.14
Mutagenesis2201C → Y in tt17; no accumulation of anthocyanin. Ref.11
Mutagenesis2281G → D in tds4-1; no accumulation of anthocyanin. Ref.6 Ref.11
Mutagenesis2301E → Q: Retains one half of the original activity. Ref.14
Mutagenesis3411K → N: Retains two-third of the original activity. Ref.14

Secondary structure

.................................................................... 356
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96323 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 1B74AE3A54056201

FASTA35640,396
        10         20         30         40         50         60 
MVAVERVESL AKSGIISIPK EYIRPKEELE SINDVFLEEK KEDGPQVPTI DLKNIESDDE 

        70         80         90        100        110        120 
KIRENCIEEL KKASLDWGVM HLINHGIPAD LMERVKKAGE EFFSLSVEEK EKYANDQATG 

       130        140        150        160        170        180 
KIQGYGSKLA NNASGQLEWE DYFFHLAYPE EKRDLSIWPK TPSDYIEATS EYAKCLRLLA 

       190        200        210        220        230        240 
TKVFKALSVG LGLEPDRLEK EVGGLEELLL QMKINYYPKC PQPELALGVE AHTDVSALTF 

       250        260        270        280        290        300 
ILHNMVPGLQ LFYEGKWVTA KCVPDSIVMH IGDTLEILSN GKYKSILHRG LVNKEKVRIS 

       310        320        330        340        350 
WAVFCEPPKD KIVLKPLPEM VSVESPAKFP PRTFAQHIEH KLFGKEQEEL VSEKND 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of flavonol synthase and leucoanthocyanidin dioxygenase genes in Arabidopsis. Further evidence for differential regulation of 'early' and 'late' genes."
Pelletier M.K., Murrell J.R., Shirley B.W.
Plant Physiol. 113:1437-1445(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY LIGHT.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Disruption of specific flavonoid genes enhances the accumulation of flavonoid enzymes and end-products in Arabidopsis seedlings."
Pelletier M.K., Burbulis I.E., Winkel-Shirley B.
Plant Mol. Biol. 40:45-54(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"The Arabidopsis TDS4 gene encodes leucoanthocyanidin dioxygenase (LDOX) and is essential for proanthocyanidin synthesis and vacuole development."
Abrahams S., Lee E., Walker A.R., Tanner G.J., Larkin P.J., Ashton A.R.
Plant J. 35:624-636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-228.
Strain: cv. Wassilewskija-4.
[7]"Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans."
Welford R.W., Kirkpatrick J.M., McNeill L.A., Puri M., Oldham N.J., Schofield C.J.
FEBS Lett. 579:5170-5174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[8]"Sucrose-specific induction of the anthocyanin biosynthetic pathway in Arabidopsis."
Solfanelli C., Poggi A., Loreti E., Alpi A., Perata P.
Plant Physiol. 140:637-646(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY SUCROSE.
[9]"Arabidopsis thaliana expresses a second functional flavonol synthase."
Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U., Martens S.
FEBS Lett. 583:1981-1986(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Molecular mechanism for jasmonate-induction of anthocyanin accumulation in Arabidopsis."
Shan X., Zhang Y., Peng W., Wang Z., Xie D.
J. Exp. Bot. 60:3849-3860(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"Leucoanthocyanidin dioxygenase in Arabidopsis thaliana: characterization of mutant alleles and regulation by MYB-BHLH-TTG1 transcription factor complexes."
Appelhagen I., Jahns O., Bartelniewoehner L., Sagasser M., Weisshaar B., Stracke R.
Gene 484:61-68(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-78; CYS-220 AND GLY-228.
Strain: cv. Est-1, cv. Landsberg erecta and cv. Wassilewskija-4.
[12]"The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
Plant Physiol. Biochem. 0:0-0(2013)
Cited for: REVIEW, NOMENCLATURE.
[13]"Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana."
Wilmouth R.C., Turnbull J.J., Welford R.W., Clifton I.J., Prescott A.G., Schofield C.J.
Structure 10:93-103(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH DIHYDROQUERCETIN; 2-OXOGLUTARATE AND IRON ION.
[14]"Structural and mechanistic studies on anthocyanidin synthase catalysed oxidation of flavanone substrates: the effect of C-2 stereochemistry on product selectivity and mechanism."
Welford R.W., Clifton I.J., Turnbull J.J., Wilson S.C., Schofield C.J.
Org. Biomol. Chem. 3:3117-3126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-356 IN COMPLEX WITH NARINGENIN; 2-OXOGLUTARATE AND IRON ION, FUNCTION, MUTAGENESIS OF LYS-128; ASN-131; TYR-142; GLU-230 AND LYS-341.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70478 mRNA. Translation: AAB09572.1.
AL031018 Genomic DNA. Translation: CAA19803.1.
AL161558 Genomic DNA. Translation: CAB79243.1.
CP002687 Genomic DNA. Translation: AEE84672.1.
CP002687 Genomic DNA. Translation: AEE84673.1.
AY088203 mRNA. Translation: AAM65745.1.
PIRT05119.
RefSeqNP_001031700.1. NM_001036623.1.
NP_194019.1. NM_118417.1.
UniGeneAt.2369.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GP4X-ray2.10A1-356[»]
1GP5X-ray2.20A1-356[»]
1GP6X-ray1.75A1-356[»]
2BRTX-ray2.20A2-356[»]
ProteinModelPortalQ96323.
SMRQ96323. Positions 2-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G22880.1-P.

Proteomic databases

PaxDbQ96323.
PRIDEQ96323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G22880.1; AT4G22880.1; AT4G22880.
AT4G22880.2; AT4G22880.2; AT4G22880.
GeneID828387.
KEGGath:AT4G22880.

Organism-specific databases

TAIRAT4G22880.

Phylogenomic databases

eggNOGCOG3491.
HOGENOMHOG000276735.
InParanoidQ96323.
KOK05277.
OMARTHANDH.
PhylomeDBQ96323.
ProtClustDBPLN03178.

Enzyme and pathway databases

BioCycARA:AT4G22880-MONOMER.
ARA:GQT-1369-MONOMER.
UniPathwayUPA00009.

Gene expression databases

GenevestigatorQ96323.

Family and domain databases

Gene3D2.60.120.330. 1 hit.
InterProIPR026992. DIOX_N.
IPR027443. IPNS-like.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
PF14226. DIOX_N. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96323.

Entry information

Entry nameLDOX_ARATH
AccessionPrimary (citable) accession number: Q96323
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names