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Q96323 (LDOX_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 97. 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
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
Gene names
Name:LDOX
Ordered Locus Names:At4g22880
ORF Names:F7H19.60
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

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

General annotation (Comments)

Function

Oxidation of leucoanthocyanidins into anthocyanidins.

Catalytic activity

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

Cofactor

Binds 1 ascorbate molecule per subunit.

Binds 1 iron ion per subunit.

Pathway

Pigment biosynthesis; anthocyanin biosynthesis.

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

Sites

Metal binding2321Iron
Metal binding2341Iron
Metal binding2881Iron

Secondary structure

1 ................................................................... 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: 9112784] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 10617198] [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]"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: 11796114] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+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.
IPIIPI00525167.
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...

Protein-protein interaction databases

STRINGQ96323.

Proteomic databases

PRIDEQ96323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G22880.1; AT4G22880.1; AT4G22880.
AT4G22880.2; AT4G22880.2; AT4G22880.
GeneID828387.
GenomeReviewsGene locus AT4G22880 in contig CT486007_GR.
KEGGath:AT4G22880.
NMPDRfig|3702.1.peg.20150.

Organism-specific databases

TAIRAt4g22880.

Phylogenomic databases

GeneTreeEPGT00070000028021.
HOGENOMHBG749762.
InParanoidQ96323.
OMAVPTIDLK.
PhylomeDBQ96323.
ProtClustDBPLN03178.

Gene expression databases

GenevestigatorQ96323.
GermOnlineAT4G22880. Arabidopsis thaliana.

Family and domain databases

InterProIPR005123. Oxoglutarate/Fe-dep_oxygenase.
[Graphical view]
KOK05277.
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

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: December 14, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents