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Database: UniProt
Entry: K9SS97_9SYNE
LinkDB: K9SS97_9SYNE
Original site: K9SS97_9SYNE 
ID   K9SS97_9SYNE            Unreviewed;       253 AA.
AC   K9SS97;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=2-phytyl-1,4-naphtoquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_01982};
DE            EC=2.1.1.329 {ECO:0000256|HAMAP-Rule:MF_01982};
DE   AltName: Full=Demethylphylloquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_01982};
GN   Name=menG {ECO:0000256|HAMAP-Rule:MF_01982};
GN   ORFNames=Syn7502_00638 {ECO:0000313|EMBL:AFY72786.1};
OS   Synechococcus sp. PCC 7502.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY72786.1, ECO:0000313|Proteomes:UP000010385};
RN   [1] {ECO:0000313|EMBL:AFY72786.1, ECO:0000313|Proteomes:UP000010385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY72786.1,
RC   ECO:0000313|Proteomes:UP000010385};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methyltransferase required for the conversion of 2-
CC       phytyl-1,4-beta-naphthoquinol to phylloquinol. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01982};
CC   -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01982}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_01982}.
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DR   EMBL; CP003594; AFY72786.1; -; Genomic_DNA.
DR   RefSeq; WP_015167445.1; NC_019702.1.
DR   AlphaFoldDB; K9SS97; -.
DR   STRING; 1173263.Syn7502_00638; -.
DR   KEGG; synp:Syn7502_00638; -.
DR   PATRIC; fig|1173263.3.peg.655; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_037990_0_0_3; -.
DR   OrthoDB; 9808140at2; -.
DR   UniPathway; UPA00995; -.
DR   Proteomes; UP000010385; 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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01982}; Reference proteome {ECO:0000313|Proteomes:UP000010385};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01982};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01982}; Ubiquinone {ECO:0000313|EMBL:AFY72786.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  28542 MW;  7200533D0AAF2811 CRC64;
     MISDFVASSE QTSQQLSQQP SQQEVQELFN QIAPMYDRLN DWLSLGQHRV WKKMAIAWTN
     PKAGDTYLDL CCGSGDVAMM LARKIANKNH TGQVFGVDFS ESQLAIACHR TQSLPHLQPY
     LTWQQGDALH LEFPDQTFDG ATLSYGLRNV LDIPKCLAEL YRVLKPKAVV AILDFHRPSN
     PQTQQFQQFY LNNLVVPIAK LWNLEQEYAY LMPSLQRFPI GSDQVKLAIA SGFSKATHYP
     ILAGLMGILV LTK
//
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