ID A0A251R333_PRUPE Unreviewed; 295 AA.
AC A0A251R333;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=2-phytyl-1,4-beta-naphthoquinone methyltransferase, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03192};
DE EC=2.1.1.329 {ECO:0000256|HAMAP-Rule:MF_03192};
DE AltName: Full=Demethylphylloquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_03192};
DE AltName: Full=Menaquinone biosynthesis methyltransferase ubiE-like protein {ECO:0000256|HAMAP-Rule:MF_03192};
GN Name=MENG {ECO:0000256|HAMAP-Rule:MF_03192};
GN ORFNames=PRUPE_1G249500 {ECO:0000313|EMBL:ONI30406.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI30406.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI30406.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- FUNCTION: Involved in the biosynthesis of phylloquinone (vitamin K1).
CC Methyltransferase required for the conversion of 2-phytyl-1,4-beta-
CC naphthoquinol to phylloquinol. {ECO:0000256|HAMAP-Rule:MF_03192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=demethylphylloquinol + S-adenosyl-L-methionine = H(+) +
CC phylloquinol + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:40551,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28433, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:87844; EC=2.1.1.329;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03192};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_03192}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_03192}.
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DR EMBL; CM007651; ONI30406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251R333; -.
DR STRING; 3760.A0A251R333; -.
DR EnsemblPlants; ONI30406; ONI30406; PRUPE_1G249500.
DR Gramene; ONI30406; ONI30406; PRUPE_1G249500.
DR eggNOG; KOG1540; Eukaryota.
DR Proteomes; UP000006882; Chromosome g1.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01982; MenG_phylloquinone_subfam; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR032904; MenG.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR NCBIfam; TIGR01934; MenG_MenH_UbiE; 1.
DR PANTHER; PTHR43591; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43591:SF106; METHYLTRANSFERASE-LIKE PROTEIN 27; 1.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01183; UBIE_1; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|HAMAP-Rule:MF_03192};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03192}; Plastid {ECO:0000256|HAMAP-Rule:MF_03192};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03192}.
SQ SEQUENCE 295 AA; 32713 MW; 1901B9C316F35294 CRC64;
MAHHVLDCDS LIRSLSLTKK LYLCFNVSAK EKRIADMASL QLHLLPFSTG PCLPSSRFRR
SLVRSSTKRQ ALFNRIAPVY DNLNDLLSLG QHRIWKRMAV SWSGAKKGDS VLDLCCGSGD
LAFLLSEKVG SSGKVIGLDF SKEQLSVASS RQKLMSKAFH TNIEWVEGDA IDLPFSDGHF
DAITMGYGLR NVVDKHKAMQ EMYRVSKAGS RVSILDFNKS INPVIAFTQE LMIDNVVVPV
ASGFGLAEDY KYLKSSIREF LTGKELEELA LDVGFSNARY YEIGGSLMGN LVATR
//
