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UniProtKB/Swiss-Prot entry Q96323


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LDOX_ARATH
Primary accession number Q96323
Secondary accession numbers None
Integrated into Swiss-Prot on April 23, 2003
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 71)
Name and origin of the protein
Protein name Leucoanthocyanidin dioxygenase
Synonyms LDOX
Leucocyanidin oxygenase
EC 1.14.11.19
Leucoanthocyanidin hydroxylase
Anthocyanidin synthase
ANS
Gene name
Name: LDOX
OrderedLocusNames: At4g22880
ORFNames: F7H19.60
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1104/pp.113.4.1437; PubMed=9112784 [NCBI, ExPASy, EBI, Israel, Japan]
Pelletier M.K., Murrell J.R., Shirley B.W.;
"Characterization of flavonol synthase and leucoanthocyanidin dioxygenase genes in Arabidopsis. Further evidence for differential regulation of 'early' and 'late' genes.";
Plant Physiol. 113:1437-1445(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1016/S0969-2126(01)00695-5; PubMed=11796114 [NCBI, ExPASy, EBI, Israel, Japan]
Wilmouth R.C., Turnbull J.J., Welford R.W., Clifton I.J., Prescott A.G., Schofield C.J.;
"Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana.";
Structure 10:93-103(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U70478; AAB09572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031018; CAA19803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161558; CAB79243.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088203; AAM65745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05119; T05119.
RefSeq NP_001031700.1; -.
NP_194019.1; -.
UniGene At.2369
3D structure databases
PDB
1GP4; X-ray; 2.10 A; A=1-356.[ExPASy / RCSB / EBI]
1GP5; X-ray; 2.20 A; A=1-356.[ExPASy / RCSB / EBI]
1GP6; X-ray; 1.75 A; A=1-356.[ExPASy / RCSB / EBI]
2BRT; X-ray; 2.20 A; A=2-356.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GP4; -.
1GP5; -.
1GP6; -.
2BRT; -.
ModBase Q96323.
Organism-specific databases
TAIR At4g22880; -.
Gene expression databases
GermOnline AT4G22880; Arabidopsis thaliana.
Family and domain databases
InterPro IPR005123; 2OG-FeII_Oase.
Graphical view of domain structure.
Pfam PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.
BLOCKS Q96323.
Genome annotation databases
GeneID 828387; -.
GenomeReviews CT486007_GR; AT4G22880.
KEGG ath:AT4G22880; -.
NMPDR fig|3702.1.peg.20150; -.
Other
ProtoNet Q96323.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   356  356     Leucoanthocyanidin dioxygenase. PRO_0000067299
METAL   232   232        Iron. 
METAL   234   234        Iron. 
METAL   288   288        Iron. 
HELIX   7    11  5      
TURN   12    14  3      
HELIX   20    22  3      
HELIX   26    29  4      
HELIX   35    40  6      
STRAND   49    51  3      
TURN   53    56  4      
HELIX   60    76  17      
STRAND   78    84  7      
HELIX   89   103  15      
HELIX   107   110  4      
HELIX   111   113  3      
HELIX   117   119  3      
STRAND   124   126  3      
STRAND   141   149  9      
HELIX   150   152  3      
HELIX   155   157  3      
HELIX   165   190  26      
HELIX   197   201  5      
HELIX   204   207  4      
STRAND   209   217  9      
HELIX   223   225  3      
STRAND   228   232  5      
STRAND   236   243  8      
STRAND   249   253  5      
STRAND   256   259  4      
STRAND   267   271  5      
HELIX   273   278  6      
TURN   279   281  3      
STRAND   288   290  3      
STRAND   298   306  9      
TURN   309   311  3      
HELIX   318   320  3      
STRAND   323   325  3      
HELIX   334   346  13      
Sequence information
Length: 356 AA [This is the length of the unprocessed precursor] Molecular weight: 40396 Da [This is the MW of the unprocessed precursor] CRC64: 1B74AE3A54056201 [This is a checksum on the sequence]
        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 

Q96323 in FASTA format

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