UBIE_COXB1
ID UBIE_COXB1 Reviewed; 250 AA.
AC B6J676;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE {ECO:0000255|HAMAP-Rule:MF_01813};
DE EC=2.1.1.163 {ECO:0000255|HAMAP-Rule:MF_01813};
DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_01813};
DE AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase {ECO:0000255|HAMAP-Rule:MF_01813};
DE AltName: Full=Demethylmenaquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01813};
GN Name=ubiE {ECO:0000255|HAMAP-Rule:MF_01813}; OrderedLocusNames=CbuK_2068;
OS Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434924;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuK_Q154;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- FUNCTION: Methyltransferase required for the conversion of
CC demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of
CC 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-
CC methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01813};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC 1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01813};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01813}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01813}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_01813}.
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DR EMBL; CP001020; ACJ21167.1; -; Genomic_DNA.
DR RefSeq; WP_005769782.1; NZ_CCXO01000003.1.
DR AlphaFoldDB; B6J676; -.
DR SMR; B6J676; -.
DR KEGG; cbc:CbuK_2068; -.
DR HOGENOM; CLU_037990_0_0_6; -.
DR OMA; VRNFENL; -.
DR UniPathway; UPA00079; UER00169.
DR UniPathway; UPA00232; -.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
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:0009060; P:aerobic respiration; IEA:UniProtKB-UniRule.
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:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 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; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..250
FT /note="Ubiquinone/menaquinone biosynthesis C-
FT methyltransferase UbiE"
FT /id="PRO_1000187749"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT BINDING 122..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
SQ SEQUENCE 250 AA; 28336 MW; 184ECE39B2FA3EAF CRC64;
MNETEKSTHF GYQTVPTDQK TDKVKHVFES VAAKYDLMND LMSLGIHRWW KDFAITQCRL
RTGQRILDLA GGTGDLAKRI SPLVGDEGEV VIADINAAML NVGRRRLLDQ GIFRNIQFIQ
ADAEKLPFPN NFFDRIVIGF GLRNVTNQLA ALQSMHRVIK PGGFVVILEF SKPTLAPLKA
VYDAYSFQLL PRLGKLVAKD EESYRYLVES IRMHPDQEAL LSKMTDARFE DCDYHNLSGG
IVAVHRGYKF
