ID   MENG_TRIV2              Reviewed;         229 AA.
AC   Q3MD91;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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}; OrderedLocusNames=Ava_1422;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA21045.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MD91; -.
DR   SMR; Q3MD91; -.
DR   STRING; 240292.Ava_1422; -.
DR   EnsemblBacteria; ABA21045; ABA21045; Ava_1422.
DR   KEGG; ava:Ava_1422; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_037990_0_0_3; -.
DR   OMA; WQKSALN; -.
DR   UniPathway; UPA00995; -.
DR   Proteomes; UP000002533; Chromosome.
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..229
FT                   /note="2-phytyl-1,4-naphtoquinone methyltransferase"
FT                   /id="PRO_1000056214"
SQ   SEQUENCE   229 AA;  25841 MW;  0F15C6F981E60A1C CRC64;
     MTNEIRAIFD RIAPVYDQLN DWLSLGQHRI WKEMAIKWTG AKPGDTCLDL CCGSGDLALR
     LARRVGSTGQ VYGVDFSANL LETAKQRAQA QYPQPHISWV EANVLDLPFE DNQFDAATMG
     YGLRNVTDIP RSLQELRRVL KPNAKAAILD FHRPNNQQFR TFQQWYLDSI VVPLADRLGV
     KEEYAYISPS LDRFPIGKEQ VEIALQVGFT SATHYPIANG MMGVLIISK