LAHY_LARTR
ID LAHY_LARTR Reviewed; 584 AA.
AC Q6UIL3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=(+)-larreatricin hydroxylase, chloroplastic;
DE EC=1.14.99.47;
DE AltName: Full=Polyphenol oxidase;
DE Flags: Precursor;
OS Larrea tridentata (Creosote bush) (Zygophyllum tridentatum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Zygophyllales; Zygophyllaceae; Larreoideae; Larrea.
OX NCBI_TaxID=66636;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND PROCESSING.
RX PubMed=12960376; DOI=10.1073/pnas.1934562100;
RA Cho M.H., Moinuddin S.G., Helms G.L., Hishiyama S., Eichinger D.,
RA Davin L.B., Lewis N.G.;
RT "(+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from
RT the creosote bush (Larrea tridentata).";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10641-10646(2003).
CC -!- FUNCTION: Enantio-specific polyphenol oxidase involved in aromatic ring
CC hydroxylation. Involved in the biosynthesis of the creosote bush 8-8'
CC linked lignans. Has a strong preference for the 3' position of (+)-
CC larreatricin. {ECO:0000269|PubMed:12960376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-larreatricin + AH2 + O2 = (+)-3'-hydroxylarreatricin + A +
CC H2O; Xref=Rhea:RHEA:34259, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:67153,
CC ChEBI:CHEBI:67154; EC=1.14.99.47;
CC Evidence={ECO:0000269|PubMed:12960376};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000305|PubMed:12960376}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; AY370019; AAQ67412.1; -; mRNA.
DR AlphaFoldDB; Q6UIL3; -.
DR SMR; Q6UIL3; -.
DR BRENDA; 1.14.18.1; 8039.
DR BRENDA; 1.14.99.47; 8039.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901708; P:(+)-3'-hydroxylarreatricin biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901709; P:(+)-larreatricin metabolic process; IDA:UniProtKB.
DR GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF12142; PPO1_DWL; 1.
DR Pfam; PF12143; PPO1_KFDV; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000290; PPO_plant; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW Plastid; Thioether bond; Thylakoid; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 33..79
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN 80..584
FT /note="(+)-larreatricin hydroxylase, chloroplastic"
FT /id="PRO_0000421296"
FT PROPEP 432..584
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000421297"
FT BINDING 167
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 319
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 323
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 353
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 91..106
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 105..168
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 171..188
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ SEQUENCE 584 AA; 66352 MW; 77C31CBD6A446DF5 CRC64;
MASLSSQSKL LATPYSFPYH TKPSRVSLRR VSCKASNDNK DKPNDQEKTF SIDRRNMLIG
LGGLYGASNV FPSNQSTLAA PIQPPVLPDS CHPPEDLAEG VNVLCCPPDV KDPIDFQMPS
NPSRLRIRPA AHLADPTYIE KYKKALAAMK ALPQNDPRSF YQQANIHCAY CNGAYDQVGF
PDVNIQVHHS WLFLPFHRWY LYFYERILGS LIDDPTFAIP FWNWDAPKGM HMPHMFIDPN
SPLYDAKRNP AHFPDTIVDL DFSSGEAPSH NPRQIGNNLS IMYKQVVRAK KARLFHGRPL
QAGSFPDESG DGSLEGTPHG NIHLWSGDPR QSNFENMGNF YSAGRDPLFY AHHANVDRMW
YIWKNSLGRK DYKKKDWLNA GFLLFDENAQ PVRVYVRDAL DERKLGYAYQ EVDIPWINSK
PKPRKANPWP NRLRSKATTT TKLINKFPLT LDSTVSFEVK RPKKSRSKSE KEDEEEVLVI
EKIKHEPQFP LKFDVYINDE DEDPSAADQT EFAGSFVNVP HFHRHGDKKD KRQTTNLSIG
ISEVLDELDV DGDDSIVVTL VPRVGSGQIT IGGAKIEFVR DEED
