CLH1_ARATH
ID CLH1_ARATH Reviewed; 324 AA.
AC O22527;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Chlorophyllase-1 {ECO:0000303|PubMed:10611389};
DE Short=AtCLH1 {ECO:0000303|PubMed:10611389};
DE EC=3.1.1.14 {ECO:0000269|PubMed:10611389};
DE AltName: Full=Chlorophyll-chlorophyllido hydrolase 1 {ECO:0000305};
DE Short=Chlase 1 {ECO:0000303|PubMed:10611389};
DE AltName: Full=Coronatine-induced protein 1 {ECO:0000303|PubMed:10611389};
DE Short=CORI1 {ECO:0000303|PubMed:10611389};
GN Name=CLH1 {ECO:0000303|PubMed:10611389};
GN Synonyms=ATHCOR1 {ECO:0000303|PubMed:9501136}, COR1;
GN OrderedLocusNames=At1g19670 {ECO:0000312|Araport:AT1G19670};
GN ORFNames=F6F9.28 {ECO:0000312|EMBL:AAG12547.1};
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], INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RC TISSUE=Flower, Leaf, Seedling, and Silique;
RX PubMed=9501136; DOI=10.1104/pp.116.3.1037;
RA Benedetti C.E., Costa C.L., Turcinelli S.R., Arruda P.;
RT "Differential expression of a novel gene in response to coronatine, methyl
RT jasmonate, and wounding in the Coi1 mutant of Arabidopsis.";
RL Plant Physiol. 116:1037-1042(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 FUNCTION, AND CATALYTIC ACTIVITY.
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 [6]
RP FUNCTION, CHARACTERIZATION, AND DEVELOPMENTAL STAGE.
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 [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=15598807; DOI=10.1105/tpc.104.025817;
RA Kariola T., Brader G., Li J., Palva E.T.;
RT "Chlorophyllase 1, a damage control enzyme, affects the balance between
RT defense pathways in plants.";
RL Plant Cell 17:282-294(2005).
RN [8]
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 [9]
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 [10]
RP INDUCTION.
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 [11]
RP FUNCTION.
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, PubMed:11950974).
CC Shows a preferential activity toward chlorophyll a (PubMed:11950974).
CC Does not seem to be required for chlorophyll degradation during
CC senescence (PubMed:17996203, PubMed:18349515, PubMed:31779896). May
CC modulate the balance between different plant defense pathways
CC (PubMed:15598807). {ECO:0000269|PubMed:10611389,
CC ECO:0000269|PubMed:11950974, ECO:0000269|PubMed:15598807,
CC ECO:0000269|PubMed:17996203, ECO:0000269|PubMed:18349515,
CC 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; EC=3.1.1.14;
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 -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers and
CC siliques, but not in roots. {ECO:0000269|PubMed:9501136}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed in flowers with a higher
CC level at the stage of buds. {ECO:0000269|PubMed:11950974}.
CC -!- INDUCTION: Induced by methyl jasmonate, coronatine, a phytotoxin
CC produced by some plant-pathogenic bacteria or rapidly after wounding,
CC with a peak after 30 minutes and a return to the basal level in the
CC following 4 hours (PubMed:9501136). Induced by methyl jasmonate (JA),
CC wounding, infection with the bacterial pathogen Pectobacterium
CC carotovorum, and with the fungal pathogen Alternaria brassicicola
CC (PubMed:15598807). Induced by transition from dark to white light
CC (PubMed:21896889). Down-regulated by dark (PubMed:21896889).
CC {ECO:0000269|PubMed:15598807, ECO:0000269|PubMed:21896889,
CC ECO:0000269|PubMed:9501136}.
CC -!- MISCELLANEOUS: It has been proposed that some chlorophyllase might be
CC transported to vacuole via the endoplasmic reticulum where they might
CC be glycosylated (Probable). Unlike CLH2, the expression of this protein
CC is dependent on the presence of a functional COI1 protein
CC (PubMed:11950974). Plants silencing CLH1 exhibit reduced size, and
CC decreased levels of chlorophyll and chlorophyllide (PubMed:15598807).
CC Plants silencing CLH1 exhibit enhanced resistance and salicylate (SA)
CC levels, and decreased jasmonate levels (JA) upon infection with the
CC bacterial pathogen Pectobacterium carotovorum (PubMed:15598807). Plants
CC silencing CLH1 exhibit enhanced susceptibility to infection by the
CC fungal pathogen Alternaria brassicicola (PubMed:15598807).
CC {ECO:0000269|PubMed:11950974, ECO:0000269|PubMed:15598807,
CC ECO:0000305|PubMed:10611389}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF021244; AAC13947.1; -; mRNA.
DR EMBL; AC007797; AAG12547.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29881.1; -; Genomic_DNA.
DR EMBL; AY099815; AAM20666.1; -; mRNA.
DR EMBL; BT000309; AAN15628.1; -; mRNA.
DR PIR; E86329; E86329.
DR RefSeq; NP_564094.1; NM_101823.4.
DR AlphaFoldDB; O22527; -.
DR SMR; O22527; -.
DR BioGRID; 23793; 5.
DR IntAct; O22527; 5.
DR STRING; 3702.AT1G19670.1; -.
DR SwissLipids; SLP:000001498; -.
DR ESTHER; arath-clh1; Chlorophyllase.
DR PaxDb; O22527; -.
DR PRIDE; O22527; -.
DR ProteomicsDB; 241039; -.
DR EnsemblPlants; AT1G19670.1; AT1G19670.1; AT1G19670.
DR GeneID; 838554; -.
DR Gramene; AT1G19670.1; AT1G19670.1; AT1G19670.
DR KEGG; ath:AT1G19670; -.
DR Araport; AT1G19670; -.
DR TAIR; locus:2013129; AT1G19670.
DR eggNOG; ENOG502QT6A; Eukaryota.
DR HOGENOM; CLU_064603_0_0_1; -.
DR InParanoid; O22527; -.
DR OMA; CKNGTGP; -.
DR OrthoDB; 1174473at2759; -.
DR PhylomeDB; O22527; -.
DR BioCyc; MetaCyc:AT1G19670-MON; -.
DR BRENDA; 3.1.1.14; 399.
DR UniPathway; UPA00674; -.
DR PRO; PR:O22527; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22527; baseline and differential.
DR Genevisible; O22527; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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 GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP: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; Plant defense;
KW Reference proteome.
FT CHAIN 1..324
FT /note="Chlorophyllase-1"
FT /id="PRO_0000090386"
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 168
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9LE89"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9LE89"
SQ SEQUENCE 324 AA; 34855 MW; 46350A84978E0453 CRC64;
MAAIEDSPTF SSVVTPAAFE IGSLPTTEIP VDPVENDSTA PPKPVRITCP TVAGTYPVVL
FFHGFYLRNY FYSDVLNHIA SHGYILVAPQ LCKLLPPGGQ VEVDDAGSVI NWASENLKAH
LPTSVNANGK YTSLVGHSRG GKTAFAVALG HAATLDPSIT FSALIGIDPV AGTNKYIRTD
PHILTYKPES FELDIPVAVV GTGLGPKWNN VMPPCAPTDL NHEEFYKECK ATKAHFVAAD
YGHMDMLDDD LPGFVGFMAG CMCKNGQRKK SEMRSFVGGI VVAFLKYSLW GEKAEIRLIV
KDPSVSPAKL DPSPELEEAS GIFV
