ID F5L722_CALTT Unreviewed; 237 AA.
AC F5L722;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=CathTA2_1622 {ECO:0000313|EMBL:EGL82857.1}, HUR95_09965
GN {ECO:0000313|EMBL:QZT32711.1};
OS Caldalkalibacillus thermarum (strain TA2.A1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL82857.1, ECO:0000313|Proteomes:UP000010716};
RN [1] {ECO:0000313|EMBL:EGL82857.1, ECO:0000313|Proteomes:UP000010716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL82857.1,
RC ECO:0000313|Proteomes:UP000010716};
RX PubMed=21685297; DOI=10.1128/JB.05035-11;
RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA Cook G.M.;
RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT thermarum strain TA2.A1.";
RL J. Bacteriol. 193:4290-4291(2011).
RN [2] {ECO:0000313|EMBL:QZT32711.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT32711.1};
RX PubMed=33030592;
RA de Jong S.I., van den Broek M.A., Merkel A.Y., de la Torre Cortes P.,
RA Kalamorz F., Cook G.M., van Loosdrecht M.C.M., McMillan D.G.G.;
RT "Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic
RT alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic
RT bacteria and plant life.";
RL Extremophiles 24:923-935(2020).
RN [3] {ECO:0000313|EMBL:QZT32711.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT32711.1};
RA de Jong S., van den Broek M., Merkel A., de la Torre Cortes P.,
RA Kalamorz F., Cook G., van Loosdrecht M., McMillan D.;
RL Submitted (AUG-2021) 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; AFCE01000136; EGL82857.1; -; Genomic_DNA.
DR EMBL; CP082237; QZT32711.1; -; Genomic_DNA.
DR RefSeq; WP_007504655.1; NZ_CP082237.1.
DR AlphaFoldDB; F5L722; -.
DR KEGG; cthu:HUR95_09965; -.
DR eggNOG; COG2226; Bacteria.
DR OrthoDB; 9808140at2; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000010716; Unassembled WGS sequence.
DR Proteomes; UP000825179; Chromosome.
DR GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC.
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 GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProt.
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; 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.
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:UP000010716};
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:EGL82857.1}.
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 107..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ SEQUENCE 237 AA; 27211 MW; AFA344986BA4C706 CRC64;
MNKQSKEQFV HQVFESIADK YDMMNTLLSF RRHKAWRKFA MKKLNVQPGQ SAIDVCCGTG
DWAIALAEKT GREGRVVGLD FSKNMLEIAE QKKSEKQYDH LELVHGNAMS LPYEDHTFDY
ATIGFALRNV PDIHQVLTEM TRVVKPGGVV ASLELSKPVW PGFKQLYYLY FNRLLPFLGK
VFANRYEQYS WLPESLKHFP DSQELGRMFE TAGLEKVEIY LLTGGVAALH IGYKPRL
//
