HPL_SOLLC
ID HPL_SOLLC Reviewed; 476 AA.
AC K4CF70; Q9ARH8; Q9LLA9;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Fatty acid hydroperoxide lyase, chloroplastic {ECO:0000303|PubMed:10859201};
DE Short=LeHPL {ECO:0000303|PubMed:10859201};
DE EC=4.2.99.- {ECO:0000305};
DE AltName: Full=Cytochrome P450 74B {ECO:0000305};
GN Name=HPL {ECO:0000303|PubMed:10859201}; OrderedLocusNames=Solyc07g049690;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|Proteomes:UP000004994};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=10923789; DOI=10.1271/bbb.64.1189;
RA Matsui K., Miyahara C., Wilkinson J., Hiatt B., Knauf V., Kajiwara T.;
RT "Fatty acid hydroperoxide lyase in tomato fruits: cloning and properties of
RT a recombinant enzyme expressed in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 64:1189-1196(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBSTRATE SPECIFICITY, TISSUE
RP SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=10859201; DOI=10.1104/pp.123.2.711;
RA Howe G.A., Lee G.I., Itoh A., Li L., DeRocher A.E.;
RT "Cytochrome P450-dependent metabolism of oxylipins in tomato. Cloning and
RT expression of allene oxide synthase and fatty acid hydroperoxide lyase.";
RL Plant Physiol. 123:711-724(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Richard S., Atwal A.S.;
RT "Comparative study between fatty acid hydroperoxide lyases from tomato and
RT red bell pepper sources.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11154338; DOI=10.1104/pp.125.1.306;
RA Froehlich J.E., Itoh A., Howe G.A.;
RT "Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two
RT cytochrome P450s involved in oxylipin metabolism, are targeted to different
RT membranes of chloroplast envelope.";
RL Plant Physiol. 125:306-317(2001).
CC -!- FUNCTION: Cytochrome P450 of the CYP74B subfamily involved in the
CC biosynthesis of traumatin and C6 aldehydes (PubMed:10923789,
CC PubMed:10859201). Metabolizes 13- but not 9-hydroperoxides of linoleic
CC and linolenic acids (PubMed:10923789, PubMed:10859201). Can use 15S-
CC hydroperoxy-11(Z),13(E),17(Z)-eicosatrienoic acid (15-HPET) and 13S-
CC hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13-HPOT) as
CC substrates, but only 5% activity with 13S-hydroperoxy-9(Z),11(E)-
CC octadecadienoic acid (13-HPOD) (PubMed:10859201). Produces n-hexanal
CC and 12-oxo-9(Z)-dodecanoic acid from 13-HPOD (PubMed:10923789).
CC {ECO:0000269|PubMed:10859201, ECO:0000269|PubMed:10923789}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- ACTIVITY REGULATION: Reversibly inhibited by nordihydroguaiaretic acid
CC (NDGA) and irreversibly by salicylic acid.
CC {ECO:0000269|PubMed:10923789}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:10923789};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:11154338}; Single-pass membrane protein
CC {ECO:0000255}; Intermembrane side {ECO:0000269|PubMed:11154338}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing flowers and in young
CC leaves. Detected in stems and immature green fruits, but not in mature
CC green and red fruits. {ECO:0000269|PubMed:10859201}.
CC -!- INDUCTION: Up-regulated by wounding. {ECO:0000269|PubMed:10859201}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF230372; AAF67142.1; -; mRNA.
DR EMBL; AY028373; AAK27265.1; -; mRNA.
DR PIR; JC7304; JC7304.
DR RefSeq; NP_001234420.2; NM_001247491.2.
DR AlphaFoldDB; K4CF70; -.
DR SMR; K4CF70; -.
DR STRING; 4081.Solyc07g049690.2.1; -.
DR ChEMBL; CHEMBL4105968; -.
DR PaxDb; K4CF70; -.
DR PRIDE; K4CF70; -.
DR EnsemblPlants; Solyc07g049690.3.1; Solyc07g049690.3.1; Solyc07g049690.3.
DR GeneID; 543642; -.
DR Gramene; Solyc07g049690.3.1; Solyc07g049690.3.1; Solyc07g049690.3.
DR KEGG; sly:543642; -.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; K4CF70; -.
DR OMA; DMRVCAY; -.
DR OrthoDB; 485250at2759; -.
DR PhylomeDB; K4CF70; -.
DR Proteomes; UP000004994; Chromosome 7.
DR ExpressionAtlas; K4CF70; baseline and differential.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Oxylipin biosynthesis; Plant defense; Plastid; Plastid outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Fatty acid hydroperoxide lyase, chloroplastic"
FT /id="PRO_0000436189"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 438
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
FT CONFLICT 194
FT /note="P -> S (in Ref. 2; AAF67142)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="E -> G (in Ref. 3; AAK27265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53553 MW; BBE1A8CCF0A8C522 CRC64;
MNSAPLSTPA PVTLPVRSIP GSYGLPLVGP IADRLDYFWF QKPENFFTKR MEKHKSTVFR
TNVPPCFPFF GSVNPNVVAV LDVKSFSHLF DMEIVEKANV LVGDFMPSVV YTGDMRVCAY
LDTSEPKHAQ IKNFSQDILK RGSKTWVPTL LKELDTMFTT FEADLSKSNT ASLLPALQKF
LFNFFSLTIL GADPSVSPEI ANSGYIFLDS WLAIQLAPTV SIGVLQPLEE ILVHSFAYPF
FLVKGNYEKL VQFVKNEAKE VLSRAQTEFQ LTEQEAIHNL LFILGFNAFG GFSIFLPTLL
GNLGDEKNAD MQEKLRKEVR DKVGVNPENL SFESVKEMEL VQSFVYETLR LSPPVPSQYA
RARKDFKLSS HDSVYEIKKG ELLCGYQPLV MKDPKVFDEP EKFVLERFTK EKGKELLNYL
FWSNGPQTGR PTESNKQCAA KDMVTLTASL IVAYIFQKYD SVSFSSGSLT SVKKAS
