ID   RCCR_ARATH              Reviewed;         319 AA.
AC   Q8LDU4; O23185;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Red chlorophyll catabolite reductase, chloroplastic;
DE            Short=RCC reductase;
DE            Short=AtRCCR;
DE            EC=1.3.1.80;
DE   AltName: Full=Accelerated cell death protein 2;
DE   Flags: Precursor;
GN   Name=RCCR; Synonyms=ACD2; OrderedLocusNames=At4g37000;
GN   ORFNames=C7A10_360;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20208062; PubMed=10743659;
RX   DOI=10.1046/j.1365-313x.2000.00667.x;
RA   Wuethrich K.L., Bovet L., Hunziker P.E., Donnison I.S.,
RA   Hoertensteiner S.;
RT   "Molecular cloning, functional expression and characterization of RCC
RT   reductase, involved in chlorophyll catabolism.";
RL   Plant J. 21:189-198(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   GLY-140; 181-TYR--ASP-192 AND ARG-279.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21143384; PubMed=11149948; DOI=10.1073/pnas.021465298;
RA   Mach J.M., Castillo A.R., Hoogstraten R., Greenberg J.T.;
RT   "The Arabidopsis accelerated cell death gene ACD2 encodes red
RT   chlorophyll catabolite reductase and suppresses the spread of disease
RT   symptoms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:771-776(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the key reaction of chlorophyll catabolism,
CC       porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a
CC       primary fluorescent catabolite (pFCC). Works in a two-step
CC       reaction with pheophorbide a oxygenase (PaO) by reducing the
CC       C20/C1 double bond of the intermediate, RCC.
CC   -!- CATALYTIC ACTIVITY: Primary fluorescent chlorophyll catabolite +
CC       NADP(+) = red chlorophyll catabolite + NADPH.
CC   -!- PATHWAY: Porphyrin degradation; chlorophyll degradation.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Note=And a low
CC       amount in mitochondria of 7-day-old seedlings.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
CC       roots.
CC   -!- DEVELOPMENTAL STAGE: Present at all times of development. No
CC       change of levels during senescence or pathogen attack.
CC   -!- MISCELLANEOUS: The absence of light completely suppresses cell
CC       death in acd2 mutants.
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DR   EMBL; AF326347; AAG53980.1; -; mRNA.
DR   EMBL; Z99707; CAB16763.1; -; Genomic_DNA.
DR   EMBL; AL161590; CAB80366.1; -; Genomic_DNA.
DR   EMBL; AY045578; AAK73936.1; -; mRNA.
DR   EMBL; AY093785; AAM10401.1; -; mRNA.
DR   EMBL; AY085797; AAM63013.1; -; mRNA.
DR   IPI; IPI00538166; -.
DR   PIR; A85437; A85437.
DR   RefSeq; NP_195417.1; -.
DR   UniGene; At.4644; -.
DR   PDB; 2ZXK; X-ray; 2.50 A; A/B=40-319.
DR   PDB; 2ZXL; X-ray; 2.40 A; A/B=40-319.
DR   PDBsum; 2ZXK; -.
DR   PDBsum; 2ZXL; -.
DR   PRIDE; Q8LDU4; -.
DR   GeneID; 829854; -.
DR   GenomeReviews; CT486007_GR; AT4G37000.
DR   KEGG; ath:AT4G37000; -.
DR   NMPDR; fig|3702.1.peg.21804; -.
DR   TAIR; At4g37000; -.
DR   OMA; Q8LDU4; GWVDEAE.
DR   BRENDA; 1.3.1.80; 302.
DR   ArrayExpress; Q8LDU4; -.
DR   GermOnline; AT4G37000; Arabidopsis thaliana.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0051743; F:red chlorophyll catabolite reductase activity; IDA:TAIR.
DR   GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR   GO; GO:0009814; P:defense response, incompatible interaction; IMP:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0043067; P:regulation of programmed cell death; IMP:TAIR.
DR   InterPro; IPR009439; RCC_reductase.
DR   Pfam; PF06405; RCC_reductase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chlorophyll catabolism; Chloroplast; Coiled coil;
KW   Complete proteome; NADP; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT       1     39       Chloroplast (Potential).
FT   CHAIN        40    319       Red chlorophyll catabolite reductase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000022201.
FT   COILED      255    286       Potential.
FT   MUTAGEN     140    140       G->V: In acd2-12E13; spontaneous
FT                                spreading cell death lesions.
FT   MUTAGEN     181    192       Missing: In acd2-7; spontaneous spreading
FT                                cell death lesions.
FT   MUTAGEN     279    279       R->K: In acd2-6; spontaneous spreading
FT                                cell death lesions.
FT   CONFLICT    290    290       D -> E (in Ref. 5; AAM63013).
SQ   SEQUENCE   319 AA;  36449 MW;  A46DC65FB7452517 CRC64;
     MAMIFCNTLY SSSSPSYLSP LTSKPSRFSK NLRPRAQFQS MEDHDDHLRR KFMEFPYVSP
     TRKQLMVDLM STVENRLQSQ LLPCNLPPDV RNFNNPNGSA EASLHIRSGD KSSPIDFVIG
     SWIHCKIPTG VSLNITSISG FLNSSTKAPN FVVELIQSSS KSLVLILDLP HRKDLVLNPD
     YLKEYYQDTA LDSHRQSLLK LPEVNPYVSP SLFVRSAFSP TASMLKIDAE EEDKLEEILR
     DHVSPAAKEV LEVWLERCVK EEEEKIVVGE EERMELERRD KSFRRKSIED DLDLQFPRMF
     GEEVSSRVVH AIKEAFGVL
//