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UniProtKB/Swiss-Prot entry Q8LDU4


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

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Entry information
Entry name RCCR_ARATH
Primary accession number Q8LDU4
Secondary accession number O23185
Integrated into Swiss-Prot on May 16, 2003
Sequence was last modified on May 16, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name Red chlorophyll catabolite reductase, chloroplastic [Precursor]
Synonyms RCC reductase
AtRCCR
EC 1.3.1.80
Accelerated cell death protein 2
Gene name
Name: RCCR
Synonyms: ACD2
OrderedLocusNames: At4g37000
ORFNames: C7A10_360
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, FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=10743659 [NCBI, ExPASy, EBI, Israel, Japan]
Wuethrich K.L., Bovet L., Hunziker P.E., Donnison I.S., Hoertensteiner S.;
"Molecular cloning, functional expression and characterization of RCC reductase, involved in chlorophyll catabolism.";
Plant J. 21:189-198(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTANTS ACD2-7; ACD2-12E13 AND ACD2-6/ACD2-8.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.021465298; PubMed=11149948 [NCBI, ExPASy, EBI, Israel, Japan]
Mach J.M., Castillo A.R., Hoogstraten R., Greenberg J.T.;
"The Arabidopsis accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms.";
Proc. Natl. Acad. Sci. U.S.A. 98:771-776(2001).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
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.
Comments
  • FUNCTION: Catalyzes the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary fluorescent catabolite (pFCC). Works in a two-step reaction with pheophorbide a oxygenase (PaO) by reducing the C20/C1 double bond of the intermediate, RCC.
  • CATALYTIC ACTIVITY: Primary fluorescent chlorophyll catabolite + NADP+ = red chlorophyll catabolite + NADPH.
  • PATHWAY: Porphyrin degradation; chlorophyll degradation.
  • SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Note=And a low amount in mitochondria of 7-day-old seedlings.
  • TISSUE SPECIFICITY: Expressed in all tissues tested, including roots.
  • DEVELOPMENTAL STAGE: Present at all times of development. No change of levels during senescence or pathogen attack.
  • MISCELLANEOUS: The absence of light completely suppresses cell death in acd2 mutants.
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
AF326347; AAG53980.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99707; CAB16763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161590; CAB80366.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY045578; AAK73936.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY093785; AAM10401.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085797; AAM63013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A85437; A85437.
RefSeq NP_195417.1; -.
UniGene At.4644
3D structure databases
ModBase Q8LDU4.
Organism-specific databases
TAIR At4g37000; -.
Gene expression databases
ArrayExpress Q8LDU4; -.
GermOnline AT4G37000; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from InterPro).
GO:0016491; Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0015996; Biological process: chlorophyll catabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR009439; RCC_reductase.
Graphical view of domain structure.
Pfam PF06405; RCC_reductase; 1.
Pfam graphical view of domain structure.
ProtoNet Q8LDU4.
Genome annotation databases
GeneID 829854; -.
GenomeReviews CT486007_GR; AT4G37000.
KEGG ath:AT4G37000; -.
NMPDR fig|3702.1.peg.21804; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chlorophyll catabolism; Chloroplast; Coiled coil; Complete proteome; NADP; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    39  39     Chloroplast (Potential). 
CHAIN   40   319  280     Red chlorophyll catabolite reductase, chloroplastic. PRO_0000022201
COILED   255   286  32     Potential. 
MUTAGEN   140   140        G->V: In acd2-12E13; spontaneous spreading cell death lesions. 
MUTAGEN   181   192        Missing: In acd2-7; spontaneous spreading cell death lesions. 
MUTAGEN   279   279        R->K: In acd2-6; spontaneous spreading cell death lesions. 
CONFLICT   290   290        D -> E (in Ref. 5; AAM63013). 
Sequence information
Length: 319 AA [This is the length of the unprocessed precursor] Molecular weight: 36449 Da [This is the MW of the unprocessed precursor] CRC64: A46DC65FB7452517 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAMIFCNTLY SSSSPSYLSP LTSKPSRFSK NLRPRAQFQS MEDHDDHLRR KFMEFPYVSP 

        70         80         90        100        110        120 
TRKQLMVDLM STVENRLQSQ LLPCNLPPDV RNFNNPNGSA EASLHIRSGD KSSPIDFVIG 

       130        140        150        160        170        180 
SWIHCKIPTG VSLNITSISG FLNSSTKAPN FVVELIQSSS KSLVLILDLP HRKDLVLNPD 

       190        200        210        220        230        240 
YLKEYYQDTA LDSHRQSLLK LPEVNPYVSP SLFVRSAFSP TASMLKIDAE EEDKLEEILR 

       250        260        270        280        290        300 
DHVSPAAKEV LEVWLERCVK EEEEKIVVGE EERMELERRD KSFRRKSIED DLDLQFPRMF 

       310 
GEEVSSRVVH AIKEAFGVL 

Q8LDU4 in FASTA format

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