ID F8KYN2_PARAV Unreviewed; 247 AA.
AC F8KYN2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:CCB85987.1};
GN Synonyms=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN OrderedLocusNames=PUV_10370 {ECO:0000313|EMBL:CCB85987.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB85987.1, ECO:0000313|Proteomes:UP000000495};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UV7;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S.A., Horn M.;
RT "Unity in variety -- the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 0:0-0(2011).
RN [2] {ECO:0000313|EMBL:CCB85987.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(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; FR872580; CCB85987.1; -; Genomic_DNA.
DR RefSeq; WP_006341631.1; NC_015702.1.
DR AlphaFoldDB; F8KYN2; -.
DR STRING; 765952.PUV_10370; -.
DR KEGG; puv:PUV_10370; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_037990_0_0_0; -.
DR OrthoDB; 9808140at2; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000000495; 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.
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:UP000000495};
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 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 112..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ SEQUENCE 247 AA; 28355 MW; D4E4FE8DD7F3C412 CRC64;
MSKYTKENPE SIQKMFGSIA QNYDKTNAIL SFQMHKKWNQ ELVRHVGGYD ESEVLLDLCC
GTGDIAFTCL AQSKKKRKAY LLDFCQEMLD CAKEKSLVKG FQRHQISYLR ADAQKIPLES
ETVSLATLAY GIRNIQQPQE CFRETYRVLA PGGRFGILEL TKPQNRLLRF GHQIYLKTIL
PLLGKWLTNN REAYQYLCSS IHNFVPPSEI SRMLKEEGFQ QVTLSPLFGG IATLFICQKP
FLHTESQ
//
