ID   CLH1_CITSI              Reviewed;         329 AA.
AC   Q9MV14;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chlorophyllase-1, chloroplastic;
DE            EC=3.1.1.14;
DE   AltName: Full=Chlorophyll-chlorophyllido hydrolase 1;
DE            Short=Chlase 1;
DE   Flags: Precursor;
GN   Name=CHLASE1;
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Valencia;
RX   PubMed=10652137; DOI=10.1046/j.1365-313x.1999.00637.x;
RA   Jacob-Wilk D., Holland D., Goldschmidt E.E., Riov J., Eyal Y.;
RT   "Chlorophyll breakdown by chlorophyllase: isolation and functional
RT   expression of the chlase1 gene from ethylene-treated citrus fruit and its
RT   regulation during development.";
RL   Plant J. 20:653-661(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-32, CHARACTERIZATION, AND INDUCTION.
RX   PubMed=11607429; DOI=10.1073/pnas.90.20.9441;
RA   Trebitsh T., Goldschmidt E.E., Riov J.;
RT   "Ethylene induces de novo synthesis of chlorophyllase, a chlorophyll
RT   degrading enzyme, in Citrus fruit peel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9441-9445(1993).
RN   [3]
RP   SUBCELLULAR LOCATION.
RA   Brandis A., Vainstein A., Goldschmidt E.E.;
RT   "Distribution of chlorophyllase among components of chloroplast membranes
RT   in Citrus sinensis organs.";
RL   Plant Physiol. Biochem. 34:49-54(1996).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to
CC       yield chlorophyllide and phytol.
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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.76 uM for chlorophyll;
CC       pH dependence:
CC         Optimum pH is 7.5. Active from pH 5.0 to 9.0.;
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Active from 30 to 60
CC         degrees Celsius.;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       degradation.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|Ref.3}.
CC   -!- INDUCTION: Low constitutive expression during fruit development and no
CC       marked increase towards the later stages of maturation. Strongly
CC       induced after 24 hours of exogenous ethylene treatment and increased
CC       further up to 7 days. Gibberellin-A3 (GA3) and the cytokinin N6-
CC       benzyladenine (BA) inhibit this induction by ethylene.
CC       {ECO:0000269|PubMed:11607429}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF160869; AAF59834.1; -; mRNA.
DR   RefSeq; NP_001275819.1; NM_001288890.1.
DR   AlphaFoldDB; Q9MV14; -.
DR   SMR; Q9MV14; -.
DR   STRING; 2711.XP_006479664.1; -.
DR   ESTHER; citsi-Q9MV14; Chlorophyllase.
DR   GeneID; 102578008; -.
DR   KEGG; cit:102578008; -.
DR   eggNOG; ENOG502QT6A; Eukaryota.
DR   OrthoDB; 1174473at2759; -.
DR   BRENDA; 3.1.1.14; 1426.
DR   SABIO-RK; Q9MV14; -.
DR   UniPathway; UPA00674; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Chloroplast; Direct protein sequencing; Hydrolase;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:11607429"
FT   CHAIN           22..329
FT                   /note="Chlorophyllase-1, chloroplastic"
FT                   /id="PRO_0000017839"
FT   MOTIF           145..149
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000250|UniProtKB:Q948R1"
FT   ACT_SITE        147
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LE89"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LE89"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LE89"
SQ   SEQUENCE   329 AA;  35209 MW;  CC62BD292E6E011A CRC64;
     MAAMVDAKPA ASVQGTPLLA TATLPVFTRG IYSTKRITLE TSSPSSPPPP KPLIIVTPAG
     KGTFNVILFL HGTSLSNKSY SKIFDHIASH GFIVVAPQLY TSIPPPSATN ELNSAAEVAE
     WLPQGLQQNL PENTEANVSL VAVMGHSRGG QTAFALSLRY GFGAVIGLDP VAGTSKTTGL
     DPSILSFDSF DFSIPVTVIG TGLGGVARCI TACAPEGANH EEFFNRCKNS SRAHFVATDY
     GHMDILDDNP SDVKSWALSK YFCKNGNESR DPMRRCVSGI VVAFLKDFFY GDAEDFRQIL
     KDPSFAPIKL DSVEYIDASS MLTTTHVKV