ID A0A1I7MQ97_9MICC Unreviewed; 693 AA.
AC A0A1I7MQ97;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN04487966_109121 {ECO:0000313|EMBL:SFV24093.1};
OS Micrococcus terreus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=574650 {ECO:0000313|EMBL:SFV24093.1, ECO:0000313|Proteomes:UP000198881};
RN [1] {ECO:0000313|EMBL:SFV24093.1, ECO:0000313|Proteomes:UP000198881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7054 {ECO:0000313|EMBL:SFV24093.1,
RC ECO:0000313|Proteomes:UP000198881};
RA de Groot N.N.;
RL Submitted (OCT-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; FPCG01000009; SFV24093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7MQ97; -.
DR STRING; 574650.SAMN04487966_109121; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000198881; Unassembled WGS sequence.
DR GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; 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; 3.30.70.2450; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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; PTHR43476; 3-(3-HYDROXY-PHENYL)PROPIONATE/3-HYDROXYCINNAMIC ACID HYDROXYLASE; 1.
DR PANTHER; PTHR43476:SF3; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 3: Inferred from homology;
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01813}; Reference proteome {ECO:0000313|Proteomes:UP000198881};
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}; Ubiquinone {ECO:0000313|EMBL:SFV24093.1}.
FT DOMAIN 24..333
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 413..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 512
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 532
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 556..557
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ SEQUENCE 693 AA; 73840 MW; 024A820B3C0240FB CRC64;
MPMPTEFGGD GGGAGGDGGE LVLDTDVLVV GAGPTGLLLA ALLAQRGVSV IVLERRTQPS
AHSRGIGLHP PAVAALAAVG LEEAAVAAGI QVRTGVGVSD GRTLGELRFD HPGAQRPSIL
VLPQNQTEQL LAERVEQLAP GAVWRGMEVI GLEQDPAAGT AQLTVQTADG TERRPTARVV
VGADGAHSTV RALAGIPVTA RDWPDRYLMG DVPDTTDHGS DARIHLHAHG VVESFPLPGG
MRRWVVHTGH ELLPEDPWRL AELVHARTGE RIDPTRATMV SAFSVRRQLA QTMVSGQTVL
IGDAAHAVSP IGGQGMTLGW QDAVELAPLL AAPPDQRPDL TEFSVRRLRT ARIAARQAEV
NMVLGRALPR PARTVRDLAA RAVLASPLQR TLAWTYAMGW AGEPRHPRGV AVVGTGTNVD
PMPTEPAAQP SQPTSPDASQ ASVQPDGGSL ASPVARGERG AQVSSMFNGM ADRYDLMNLV
MTWGQEPRLV RRTVERAELP DAPRVLDLAT GTGDIALEIL RSRYAAEVVG ADFAPEMMEI
GRRRPGGDRI QWVEADAMDL PFEDESFDAV THGYLLRNVE DIPRTLAEQF RVLKPGGRMV
ALETSPAPKN ITRPFSTAYI QHVVPLMGRL ITQNPDAYEY LSSTTRAFKT PAEIAGLLED
AGFVDVGHEL HMFGTLAIHW AVKPGGAQAG QEG
//
