MENG_SYNE7
ID MENG_SYNE7 Reviewed; 233 AA.
AC Q31P90;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=2-phytyl-1,4-naphtoquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01982};
DE EC=2.1.1.329 {ECO:0000255|HAMAP-Rule:MF_01982};
DE AltName: Full=Demethylphylloquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01982};
GN Name=menG {ECO:0000255|HAMAP-Rule:MF_01982};
GN OrderedLocusNames=Synpcc7942_1099;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methyltransferase required for the conversion of 2-phytyl-
CC 1,4-beta-naphthoquinol to phylloquinol. {ECO:0000255|HAMAP-
CC Rule:MF_01982}.
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:0000255|HAMAP-Rule:MF_01982};
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01982}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_01982}.
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DR EMBL; CP000100; ABB57129.1; -; Genomic_DNA.
DR RefSeq; WP_011242762.1; NC_007604.1.
DR AlphaFoldDB; Q31P90; -.
DR SMR; Q31P90; -.
DR STRING; 1140.Synpcc7942_1099; -.
DR PRIDE; Q31P90; -.
DR EnsemblBacteria; ABB57129; ABB57129; Synpcc7942_1099.
DR KEGG; syf:Synpcc7942_1099; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_037990_0_0_3; -.
DR OMA; WQKSALN; -.
DR OrthoDB; 1431378at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1099-MON; -.
DR UniPathway; UPA00995; -.
DR GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01183; UBIE_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..233
FT /note="2-phytyl-1,4-naphtoquinone methyltransferase"
FT /id="PRO_1000056310"
SQ SEQUENCE 233 AA; 25441 MW; ADD1F2E1E93702E2 CRC64;
MSVLAPDAVE GLFDQIAPIY DNLNDQLSFG LHRLWKRMAV KWSAAKPGDR VLDLCCGSGD
LAFLLAKVVG SKGQVIGFDR SQALLSVAGD RARQLASALV IDWQRGDALD LPFPDDHFDA
ATLGYGLRNV PDIPTVLRQL QRVLKPGARA AILDMHRPYS PLLRQFQQVY LDRWVVPAAA
AQNCAAEYEY IDASLEAFPQ GQQQVALAIA AGFQRAKHYE LAAGLMGVLV VEA
