C74B2_ARATH
ID C74B2_ARATH Reviewed; 492 AA.
AC Q9ZSY9;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Linolenate hydroperoxide lyase, chloroplastic {ECO:0000305|PubMed:9701595};
DE EC=4.2.99.- {ECO:0000305|PubMed:9701595};
DE AltName: Full=Cytochrome P450 74B2 {ECO:0000305};
DE AltName: Full=Hydroperoxide lyase 1 {ECO:0000303|PubMed:9701595};
DE Flags: Precursor;
GN Name=CYP74B2 {ECO:0000305}; Synonyms=HPL1 {ECO:0000303|PubMed:9701595};
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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=9701595; DOI=10.1104/pp.117.4.1393;
RA Bate N.J., Sivasankar S., Moxon C., Riley J.M., Thompson J.E.,
RA Rothstein S.J.;
RT "Molecular characterization of an Arabidopsis gene encoding hydroperoxide
RT lyase, a cytochrome P-450 that is wound inducible.";
RL Plant Physiol. 117:1393-1400(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=16258015; DOI=10.1104/pp.105.067249;
RA Duan H., Huang M.Y., Palacio K., Schuler M.A.;
RT "Variations in CYP74B2 (hydroperoxide lyase) gene expression differentially
RT affect hexenal signaling in the Columbia and Landsberg erecta ecotypes of
RT Arabidopsis.";
RL Plant Physiol. 139:1529-1544(2005).
RN [3]
RP INDUCTION BY WOUNDING.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17163881; DOI=10.1111/j.1365-313x.2006.02946.x;
RA D'Auria J.C., Pichersky E., Schaub A., Hansel A., Gershenzon J.;
RT "Characterization of a BAHD acyltransferase responsible for producing the
RT green leaf volatile (Z)-3-hexen-1-yl acetate in Arabidopsis thaliana.";
RL Plant J. 49:194-207(2007).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=23630530; DOI=10.3389/fpls.2013.00074;
RA Scala A., Mirabella R., Mugo C., Matsui K., Haring M.A., Schuurink R.C.;
RT "E-2-hexenal promotes susceptibility to Pseudomonas syringae by activating
RT jasmonic acid pathways in Arabidopsis.";
RL Front. Plant Sci. 4:74-74(2013).
CC -!- FUNCTION: Catalyzes the conversion of (9Z,11E,15Z)-(13S)-
CC hydroperoxyoctadeca-9,11,15-trienoate to (9Z)-12-oxo-dodec-9-enoate and
CC cis-3-hexenal. Possesses low activity toward (9Z,11E)-(13S)-13-
CC hydroperoxyoctadeca-9,11-dienoate (PubMed:9701595, PubMed:16258015).
CC Required for the synthesis of the green leaf volatiles (GLVs) hexanal
CC and trans-2-hexenal (PubMed:16258015). {ECO:0000269|PubMed:16258015,
CC ECO:0000269|PubMed:9701595}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:16258015, ECO:0000269|PubMed:9701595}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:17163881,
CC ECO:0000269|PubMed:9701595}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants lacking HPL1 cannot synthesize the green leaf
CC volatiles (GLVs) hexanal and trans-2-hexenal.
CC {ECO:0000269|PubMed:16258015}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- CAUTION: In cv. Columbia, CYP74B2 (AC B3LF83) DNA sequence contains a
CC 10-bp deletion that leads to a shorter N-terminus compared to typical
CC other CYP74B subfamily members, and CYP74B2 is thought to be a non-
CC functional enzyme. Functional alleles, with full N-terminus are found
CC in cv. Landsberg erecta and cv. Wassilewskija (AC Q9ZSY9).
CC {ECO:0000269|PubMed:16258015}.
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DR EMBL; AF087932; AAC69871.1; -; mRNA.
DR PIR; T51860; T51860.
DR AlphaFoldDB; Q9ZSY9; -.
DR SMR; Q9ZSY9; -.
DR ExpressionAtlas; Q9ZSY9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
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; Heme; Iron; Lyase; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..492
FT /note="Linolenate hydroperoxide lyase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431453"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454
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"
SQ SEQUENCE 492 AA; 54876 MW; 45D4A4B0AF5675AE CRC64;
MLLRTMAATS PRPPPSTSLT SQQPPSPPSQ LPLRTMPGSY GWPLVGPLSD RLDYFWFQGP
DKFFRTRAEK YKSTVFRTNI PPTFPFFGNV NPNIVAVLDV KSFSHLFDMD LVDKRDVLIG
DFRPSLGFYG GVCVGVNLDT TEPKHAKIKG FAMETLKRSS KVWLQELRSN LNIFWGTIES
EISKNGAASY IFPLQRCIFS FLCASLAGVD ASVSPDIAEN GWKTINTWLA LQVIPTAKLG
VVPQPLEEIL LHTWPYPSLL IAGNYKKLYN FIDENAGDCL RLGQEEFRLT RDEAIQNLLF
VLGFNAYGGF SVFLPSLIGR ITGDNSGLQE RIRTEVRRVC GSGSDLNFKT VNEMELVKSV
VYETLRFNPP VPLQFARARK DFQISSHDAV FEVKKGELLC GYQPLVMRDA NVFDEPEEFK
PDRYVGETGS ELLNYLYWSN GPQTGTPSAS NKQCAAKDIV TLTASLLVAD LFLRYDTITG
DSGSIKAVVK AK
