ID   MENG_SYNY3              Reviewed;         238 AA.
AC   P72818;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 135.
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=sll1653;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA16833.1; -; Genomic_DNA.
DR   PIR; S74682; S74682.
DR   AlphaFoldDB; P72818; -.
DR   SMR; P72818; -.
DR   IntAct; P72818; 9.
DR   STRING; 1148.1651907; -.
DR   PaxDb; P72818; -.
DR   EnsemblBacteria; BAA16833; BAA16833; BAA16833.
DR   KEGG; syn:sll1653; -.
DR   eggNOG; COG2226; Bacteria.
DR   InParanoid; P72818; -.
DR   OMA; WQKSALN; -.
DR   PhylomeDB; P72818; -.
DR   BioCyc; MetaCyc:MON-13821; -.
DR   BRENDA; 2.1.1.329; 382.
DR   UniPathway; UPA00995; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IEA:InterPro.
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   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..238
FT                   /note="2-phytyl-1,4-naphtoquinone methyltransferase"
FT                   /id="PRO_0000193342"
SQ   SEQUENCE   238 AA;  26072 MW;  FF4110214F8053F2 CRC64;
     MSNSLLTQPT QESVQQIFAR IAPQYDDLNT FLSFGQHHIW KAMAVKWSGV SPGDRLLDVC
     CGSGDLAFQG AKVVGTRGKV VGLDFCAELL AIAAGKHKSK YAHLPMQWLQ GDALALPFSD
     NEFDGATMGY GLRNVGNIPQ ALTELQRVLK PGKKVAILDF HQPGNALAAN FQRWYLANVV
     VPMAKQWRLT EEYAYLQPSL DRFPTGPKQV QFALEVGFAK AVHYPIAAGL MGVLVAEK