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Database: UniProt
Entry: A0A0H3E2Z3_BACA1
LinkDB: A0A0H3E2Z3_BACA1
Original site: A0A0H3E2Z3_BACA1 
ID   A0A0H3E2Z3_BACA1        Unreviewed;       233 AA.
AC   A0A0H3E2Z3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=ubiE {ECO:0000313|EMBL:ADP32782.1};
GN   Synonyms=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN   OrderedLocusNames=BATR1942_09245 {ECO:0000313|EMBL:ADP32782.1};
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP32782.1, ECO:0000313|Proteomes:UP000006867};
RN   [1] {ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA   Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA   Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA   Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA   Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADP32782.1, ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|EMBL:ADP32782.1,
RC   ECO:0000313|Proteomes:UP000006867};
RX   PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA   Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA   Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA   Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA   Skowronski E.W.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus var. globigii, a historical biowarfare simulant.";
RL   PLoS ONE 6:E17836-E17836(2011).
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; CP002207; ADP32782.1; -; Genomic_DNA.
DR   RefSeq; WP_004429755.1; NC_014639.1.
DR   AlphaFoldDB; A0A0H3E2Z3; -.
DR   GeneID; 23410308; -.
DR   KEGG; bae:BATR1942_09245; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_037990_0_0_9; -.
DR   OMA; MNDVMSM; -.
DR   OrthoDB; 9808140at2; -.
DR   UniPathway; UPA00079; UER00169.
DR   Proteomes; UP000006867; Chromosome.
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};
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:ADP32782.1}.
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;  26707 MW;  04C3405317967C03 CRC64;
     MQESKEQRVH GVFEKIYKNY DQMNSVISFQ QHKKWREKTM RIMDVKEGAK ALDVCCGTAD
     WTIALAEAAG KTGEVKGLDF SKNMLSIGEK KVKDGGYSQI ELLHGNAMEL PFDDDSFDYV
     TIGFGLRNVP DYLTVLKEMR RVVKPGGQVV CLETSQPEMF GFKQAYFMYF KYIMPFFGKL
     FAKSYKEYSW LQESAREFPG MKELARLFEE AGLKNVKYHS FTGGVAATHI GWK
//
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