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Database: UniProt
Entry: A0A1M7J3L8_9SPHI
LinkDB: A0A1M7J3L8_9SPHI
Original site: A0A1M7J3L8_9SPHI 
ID   A0A1M7J3L8_9SPHI        Unreviewed;       243 AA.
AC   A0A1M7J3L8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Demethylmenaquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.163 {ECO:0000256|HAMAP-Rule:MF_01813};
GN   Name=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN   ORFNames=SAMN05216524_102234 {ECO:0000313|EMBL:SHM47659.1};
OS   Mucilaginibacter sp. OK098.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHM47659.1, ECO:0000313|Proteomes:UP000184158};
RN   [1] {ECO:0000313|EMBL:SHM47659.1, ECO:0000313|Proteomes:UP000184158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK098 {ECO:0000313|EMBL:SHM47659.1,
RC   ECO:0000313|Proteomes:UP000184158};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methyltransferase required for the conversion of
CC       demethylmenaquinol (DMKH2) to menaquinol (MKH2). {ECO:0000256|HAMAP-
CC       Rule:MF_01813}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a
CC         menaquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42640,
CC         Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18151, ChEBI:CHEBI:55437, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.163; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01813};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC       menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01813}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_01813}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01813}.
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DR   EMBL; FRCM01000002; SHM47659.1; -; Genomic_DNA.
DR   RefSeq; WP_073402255.1; NZ_FRCM01000002.1.
DR   AlphaFoldDB; A0A1M7J3L8; -.
DR   STRING; 1855297.SAMN05216524_102234; -.
DR   OrthoDB; 9808140at2; -.
DR   UniPathway; UPA00079; UER00169.
DR   Proteomes; UP000184158; Unassembled WGS sequence.
DR   GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0102094; F:S-adenosylmethionine:2-demethylmenaquinol methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102955; F:S-adenosylmethionine:2-demethylmenaquinol-7 methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102027; F:S-adenosylmethionine:2-demethylquinol-8 methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
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:SF24; 2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43591; METHYLTRANSFERASE; 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.
DR   PROSITE; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
KW   Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW   Rule:MF_01813};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01813};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01813};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01813}.
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         116..117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ   SEQUENCE   243 AA;  27231 MW;  310B6688F4D00B54 CRC64;
     MSKIITPYAD QQGTKKEQVA DMFNNISKTY DFLNHFMSLG IDIIWRKKAI NELKKDQPKL
     ILDVATGTGD FAFEALTILK PEKIIGVDIS QGMLDIAQQK IDKRNLGDKF EIKLGDSEKL
     PFDADGFDAV TVAYGVRNFE NLETGLADIH RVLKPGGKAV VLEFSKPKAF PIKQLYNFYF
     NYITPGIGKL FSKDARAYTY LPESVAAFPD GKTFTALMDK VGFKHTKHRP LAFGICSIYT
     GIK
//
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