CLH2_ARATH
ID CLH2_ARATH Reviewed; 318 AA.
AC Q9M7I7;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Chlorophyllase-2 {ECO:0000303|PubMed:10611389};
DE Short=AtCLH2 {ECO:0000303|PubMed:10611389};
DE EC=3.1.1.14 {ECO:0000269|PubMed:10611389};
DE AltName: Full=Chlorophyll-chlorophyllido hydrolase 2 {ECO:0000305};
DE Short=Chlase 2 {ECO:0000303|PubMed:10611389};
GN Name=CLH2 {ECO:0000303|PubMed:10611389}; OrderedLocusNames=At5g43860;
GN ORFNames=MQD19.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=10611389; DOI=10.1073/pnas.96.26.15362;
RA Tsuchiya T., Ohta H., Okawa K., Iwamatsu A., Shimada H., Masuda T.,
RA Takamiya K.;
RT "Cloning of chlorophyllase, the key enzyme in chlorophyll degradation:
RT finding of a lipase motif and the induction by methyl jasmonate.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15362-15367(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-318.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP CHARACTERIZATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11950974; DOI=10.1104/pp.010813;
RA Benedetti C.E., Arruda P.;
RT "Altering the expression of the chlorophyllase gene ATHCOR1 in transgenic
RT Arabidopsis caused changes in the chlorophyll-to-chlorophyllide ratio.";
RL Plant Physiol. 128:1255-1263(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17996203; DOI=10.1016/j.febslet.2007.10.060;
RA Schenk N., Schelbert S., Kanwischer M., Goldschmidt E.E., Doermann P.,
RA Hoertensteiner S.;
RT "The chlorophyllases AtCLH1 and AtCLH2 are not essential for senescence-
RT related chlorophyll breakdown in Arabidopsis thaliana.";
RL FEBS Lett. 581:5517-5525(2007).
RN [7]
RP FUNCTION.
RX PubMed=18349515;
RA Zhou X., Liao Y., Ren G.D., Zhang Y.Y., Chen W.J., Kuai B.K.;
RT "Repression of AtCLH1 expression results in a decrease in the ratio of
RT chlorophyll a/b but doesnot affect the rate of chlorophyll degradation
RT during leaf senescence.";
RL Zhi Wu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao 33:596-606(2007).
RN [8]
RP INDUCTION BY LIGHT.
RX PubMed=21896889; DOI=10.1104/pp.111.185504;
RA Banas A.K., Labuz J., Sztatelman O., Gabrys H., Fiedor L.;
RT "Expression of enzymes involved in chlorophyll catabolism in Arabidopsis is
RT light controlled.";
RL Plant Physiol. 157:1497-1504(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31779896; DOI=10.1016/j.plantsci.2019.110314;
RA Hu X., Jia T., Hoertensteiner S., Tanaka A., Tanaka R.;
RT "Subcellular localization of chlorophyllase2 reveals it is not involved in
RT chlorophyll degradation during senescence in Arabidopsis thaliana.";
RL Plant Sci. 290:110314-110314(2020).
CC -!- FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to
CC yield chlorophyllide and phytol (PubMed:10611389). Does not seem to be
CC required for chlorophyll degradation during senescence
CC (PubMed:17996203, PubMed:18349515, PubMed:31779896).
CC {ECO:0000269|PubMed:10611389, ECO:0000269|PubMed:17996203,
CC ECO:0000269|PubMed:18349515, ECO:0000269|PubMed:31779896}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a chlorophyll + H2O = a chlorophyllide + H(+) + phytol;
CC Xref=Rhea:RHEA:19605, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17327, ChEBI:CHEBI:139291, ChEBI:CHEBI:139292;
CC EC=3.1.1.14; Evidence={ECO:0000269|PubMed:10611389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19606;
CC Evidence={ECO:0000269|PubMed:10611389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyll a + H2O = chlorophyllide a + H(+) + phytol;
CC Xref=Rhea:RHEA:38011, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17327, ChEBI:CHEBI:58416, ChEBI:CHEBI:83348;
CC Evidence={ECO:0000269|PubMed:10611389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38012;
CC Evidence={ECO:0000269|PubMed:10611389};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC degradation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17996203,
CC ECO:0000269|PubMed:31779896}. Note=Associates with the tonoplast and
CC endoplasmic reticulum. {ECO:0000269|PubMed:31779896}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and flower buds, but
CC not in roots. {ECO:0000269|PubMed:11950974}.
CC -!- INDUCTION: Constitutively expressed at low level (PubMed:11950974). Not
CC induced by methyl jasmonate treatment (PubMed:11950974). Induced by
CC transition from dark to white light (PubMed:21896889).
CC {ECO:0000269|PubMed:11950974, ECO:0000269|PubMed:21896889}.
CC -!- MISCELLANEOUS: Unlike CLH1, the expression of this protein is not
CC dependent on the presence of a functional COI1 protein.
CC {ECO:0000269|PubMed:11950974}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF134302; AAF27046.1; -; mRNA.
DR EMBL; AB026651; BAB11315.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95018.1; -; Genomic_DNA.
DR EMBL; BT002898; AAO22714.1; -; mRNA.
DR RefSeq; NP_199199.1; NM_123753.3.
DR AlphaFoldDB; Q9M7I7; -.
DR SMR; Q9M7I7; -.
DR STRING; 3702.AT5G43860.1; -.
DR SwissLipids; SLP:000001499; -.
DR ESTHER; arath-clh2; Chlorophyllase.
DR PaxDb; Q9M7I7; -.
DR PRIDE; Q9M7I7; -.
DR ProteomicsDB; 246734; -.
DR EnsemblPlants; AT5G43860.1; AT5G43860.1; AT5G43860.
DR GeneID; 834408; -.
DR Gramene; AT5G43860.1; AT5G43860.1; AT5G43860.
DR KEGG; ath:AT5G43860; -.
DR Araport; AT5G43860; -.
DR TAIR; locus:2170852; AT5G43860.
DR eggNOG; ENOG502QRKW; Eukaryota.
DR HOGENOM; CLU_064603_0_0_1; -.
DR InParanoid; Q9M7I7; -.
DR OMA; RKPMRRF; -.
DR OrthoDB; 1174473at2759; -.
DR PhylomeDB; Q9M7I7; -.
DR BioCyc; ARA:AT5G43860-MON; -.
DR BioCyc; MetaCyc:AT5G43860-MON; -.
DR BRENDA; 3.1.1.14; 399.
DR UniPathway; UPA00674; -.
DR PRO; PR:Q9M7I7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M7I7; baseline and differential.
DR Genevisible; Q9M7I7; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0047746; F:chlorophyllase activity; IDA:TAIR.
DR GO; GO:0102293; F:pheophytinase b activity; IEA:UniProtKB-EC.
DR GO; GO:0015996; P:chlorophyll catabolic process; IDA:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR017395; Chlorophyllase.
DR Pfam; PF07224; Chlorophyllase; 1.
DR PIRSF; PIRSF038128; Chlorophyllase_chloroplast; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chlorophyll catabolism; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..318
FT /note="Chlorophyllase-2"
FT /id="PRO_0000017836"
FT MOTIF 136..140
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 138
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LE89"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9LE89"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9LE89"
FT CONFLICT 27
FT /note="R -> C (in Ref. 4; AAO22714)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="P -> A (in Ref. 4; AAO22714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 34904 MW; DC3EF39D7D70EB65 CRC64;
MSSSSSRNAF EDGKYKSNLL TLDSSSRCCK ITPSSRASPS PPKQLLVATP VEEGDYPVVM
LLHGYLLYNS FYSQLMLHVS SHGFILIAPQ LYSIAGPDTM DEIKSTAEIM DWLSVGLNHF
LPAQVTPNLS KFALSGHSRG GKTAFAVALK KFGYSSNLKI STLIGIDPVD GTGKGKQTPP
PVLAYLPNSF DLDKTPILVI GSGLGETARN PLFPPCAPPG VNHREFFREC QGPAWHFVAK
DYGHLDMLDD DTKGIRGKSS YCLCKNGEER RPMRRFVGGL VVSFLKAYLE GDDRELVKIK
DGCHEDVPVE IQEFEVIM
