CLH0_CHEAL
ID CLH0_CHEAL Reviewed; 347 AA.
AC Q9LE89;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Chlorophyllase type 0 {ECO:0000303|PubMed:10611389};
DE EC=3.1.1.14 {ECO:0000269|PubMed:12552153};
DE AltName: Full=CaCLH0 {ECO:0000305};
DE AltName: Full=Chlorophyll-chlorophyllido hydrolase 0 {ECO:0000305};
DE Short=Chlase 0 {ECO:0000305};
DE Flags: Precursor;
GN Name=CACLH {ECO:0000303|PubMed:10611389};
OS Chenopodium album (Fat-hen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Chenopodium.
OX NCBI_TaxID=3559;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-51; 156-166 AND 250-256,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Leaf;
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-81; HIS-100; HIS-161; SER-162; SER-167; ASP-191;
RP CYS-234; HIS-241; CYS-248; HIS-254; HIS-262; ASP-264 AND CYS-282.
RX PubMed=12552153; DOI=10.1093/pcp/pcg011;
RA Tsuchiya T., Suzuki T., Yamada T., Shimada H., Masuda T., Ohta H.,
RA Takamiya K.;
RT "Chlorophyllase as a serine hydrolase: identification of a putative
RT catalytic triad.";
RL Plant Cell Physiol. 44:96-101(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to
CC yield chlorophyllide and phytol. {ECO:0000269|PubMed:10611389,
CC ECO:0000269|PubMed:12552153}.
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:12552153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19606;
CC Evidence={ECO:0000269|PubMed:12552153};
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 -!- ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate (DFP),
CC phenylmethanesulfonyl fluoride (PMSF) or p-chloromercuribenzoic acid
CC (PCMB), but not by N-ethylmaleimide (NEM) or iodoacetamide.
CC {ECO:0000269|PubMed:12552153}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC degradation.
CC -!- MISCELLANEOUS: It has been proposed that CaCLH0 is transported to
CC vacuole via the endoplasmic reticulum where it might be glycosylated.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB025025; BAA93635.1; -; mRNA.
DR EMBL; AF134301; AAF27045.1; -; mRNA.
DR AlphaFoldDB; Q9LE89; -.
DR SwissLipids; SLP:000001500; -.
DR ESTHER; cheal-CACLH; Chlorophyllase.
DR KEGG; ag:AAF27045; -.
DR BRENDA; 3.1.1.14; 1304.
DR UniPathway; UPA00674; -.
DR GO; GO:0047746; F:chlorophyllase activity; IDA:UniProtKB.
DR GO; GO:0102293; F:pheophytinase b activity; IEA:UniProtKB-EC.
DR GO; GO:0015996; P:chlorophyll catabolic process; IDA:UniProtKB.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Chlorophyll catabolism; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..30
FT /evidence="ECO:0000250"
FT /id="PRO_0000017837"
FT CHAIN 31..347
FT /note="Chlorophyllase type 0"
FT /id="PRO_0000017838"
FT MOTIF 160..164
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:12552153"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12552153"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12552153"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 81
FT /note="H->A: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 100
FT /note="H->A: Severe loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 161
FT /note="H->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 162
FT /note="S->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 167
FT /note="S->A: Slight reduction of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 191
FT /note="D->N: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 234
FT /note="C->A: Severe loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 241
FT /note="H->A: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 248
FT /note="C->A: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 254
FT /note="H->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 254
FT /note="H->Y: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 262
FT /note="H->A,Y: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 264
FT /note="D->N: Severe loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
FT MUTAGEN 282
FT /note="C->A: Severe loss of activity."
FT /evidence="ECO:0000269|PubMed:12552153"
SQ SEQUENCE 347 AA; 38707 MW; 03EB2C5B8259B863 CRC64;
MAKLLLLIFG VFIFVNSQAQ TFPTILEKHN SEKITDVFHK GNFQVTNNPI RVKRYEFSAP
EPLIIISPKE AGVYPVLLFI HGTMLSNEDY SLFFNYIASH GFIVVAPKLF RLFPPKLPSQ
QDEIDMAASV ANWMPLYLQV VLQRYVTGVE GDLEKLAISG HSRGGKSAFA LALGFSNIKL
DVTFSALIGV DPVAGRSVDD RTLPHVLTYK PNSFNLSIPV TVIGSGLGNH TISCAPNHVS
HQQFYDECKE NSSHFVITKY GHMDMLNEFR LSPIAVTMSL MCAQSFRPKA TMRRTLGGIM
VAFLNAYFRD DGRQYYAIIA NRSLAPTNLF AEKKGFNFGF ATTYAQL
