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Entry: A0A1X7D458_9BACI
LinkDB: A0A1X7D458_9BACI
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ID   A0A1X7D458_9BACI        Unreviewed;       233 AA.
AC   A0A1X7D458; A0A0H4KNP4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-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=B1B01_03105 {ECO:0000313|EMBL:OXS71316.1}, BEH_18875
GN   {ECO:0000313|EMBL:AKO93969.1}, CJ485_20465
GN   {ECO:0000313|EMBL:RJS66957.1}, SAMN06296056_101637
GN   {ECO:0000313|EMBL:SMF08011.1};
OS   Priestia filamentosa.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1402861 {ECO:0000313|EMBL:SMF08011.1, ECO:0000313|Proteomes:UP000192915};
RN   [1] {ECO:0000313|EMBL:AKO93969.1, ECO:0000313|Proteomes:UP000036202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hbe603 {ECO:0000313|EMBL:AKO93969.1,
RC   ECO:0000313|Proteomes:UP000036202};
RX   PubMed=26248285;
RA   Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT   "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT   Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL   PLoS ONE 10:E0135104-E0135104(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA   Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT   "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT   Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AKO93969.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hbe603 {ECO:0000313|EMBL:AKO93969.1};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000215399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA   Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT   "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:SMF08011.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS71316.1}, and SGD-14
RC   {ECO:0000313|EMBL:SMF08011.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|Proteomes:UP000192915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-14 {ECO:0000313|Proteomes:UP000192915};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:RJS66957.1, ECO:0000313|Proteomes:UP000274910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PK5_39 {ECO:0000313|EMBL:RJS66957.1,
RC   ECO:0000313|Proteomes:UP000274910};
RA   Bokhari A., Bougouffa S., Essack M., Andres-Barrao C., Saad M., Bajic V.B.,
RA   Hirt H.;
RT   "Complete genomes of four Endophytic plant-growth promoting Bacillus that
RT   were isolated from a desert in Pakistan.";
RL   Submitted (AUG-2017) 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; CP011974; AKO93969.1; -; Genomic_DNA.
DR   EMBL; MWSI01000001; OXS71316.1; -; Genomic_DNA.
DR   EMBL; NQYF01000001; RJS66957.1; -; Genomic_DNA.
DR   EMBL; FXAJ01000001; SMF08011.1; -; Genomic_DNA.
DR   RefSeq; WP_019391679.1; NZ_NQYF01000001.1.
DR   AlphaFoldDB; A0A1X7D458; -.
DR   KEGG; beo:BEH_18875; -.
DR   PATRIC; fig|135735.6.peg.4005; -.
DR   OrthoDB; 9808140at2; -.
DR   UniPathway; UPA00079; UER00169.
DR   Proteomes; UP000036202; Chromosome.
DR   Proteomes; UP000192915; Unassembled WGS sequence.
DR   Proteomes; UP000215399; Unassembled WGS sequence.
DR   Proteomes; UP000274910; 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; IPR014122; MenG_heptapren.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR   InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR   NCBIfam; TIGR02752; MenG_heptapren; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000036202};
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         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         106..107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ   SEQUENCE   233 AA;  26766 MW;  3B3DD3E6642B5421 CRC64;
     MRESKEERVH KVFENISEHY DQMNSVISFR QHKLWRKDTM KRMNVKKGSR SLDVCCGTAD
     WTLAMAEAVG EQGEAIGLDF SQNMLSIGEK KVKASPYTNV SLIHGNAMEL PFEDNSFDYV
     TIGFGLRNVP DYLQVLKEMH RVLKPGGKAV CLETSQPTLI GYRQLYYFYF KRIMPLFGKL
     FAKSYEEYSW LQESAKDFPD RRALKRLFEE AGFEKINVKG YAGGAAAMHM GIK
//
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