UBIE_ECOLI
ID UBIE_ECOLI Reviewed; 251 AA.
AC P0A887; P27851; Q2M8D8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
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, ECO:0000269|PubMed:9045837};
DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_01813, ECO:0000269|PubMed:9045837};
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, ECO:0000303|PubMed:9045837};
GN Synonyms=yigO; OrderedLocusNames=b3833, JW5581;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION TO 101.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTANT UBIE401.
RX PubMed=9045837; DOI=10.1128/jb.179.5.1748-1754.1997;
RA Lee P.T., Hsu A.Y., Ha H.T., Clarke C.F.;
RT "A C-methyltransferase involved in both ubiquinone and menaquinone
RT biosynthesis: isolation and identification of the Escherichia coli ubiE
RT gene.";
RL J. Bacteriol. 179:1748-1754(1997).
RN [6]
RP FUNCTION.
RX PubMed=26023160; DOI=10.1105/tpc.15.00103;
RA Fatihi A., Latimer S., Schmollinger S., Block A., Dussault P.H.,
RA Vermaas W.F., Merchant S.S., Basset G.J.;
RT "A dedicated type II NADPH dehydrogenase performs the penultimate step in
RT the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis.";
RL Plant Cell 27:1730-1741(2015).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=30686758; DOI=10.1016/j.chembiol.2018.12.001;
RA Hajj Chehade M., Pelosi L., Fyfe C.D., Loiseau L., Rascalou B.,
RA Brugiere S., Kazemzadeh K., Vo C.D., Ciccone L., Aussel L., Coute Y.,
RA Fontecave M., Barras F., Lombard M., Pierrel F.;
RT "A soluble metabolon synthesizes the isoprenoid lipid ubiquinone.";
RL Cell Chem. Biol. 26:482-492(2019).
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) (PubMed:9045837). In vitro,
CC can use demethylphylloquinol, an intermediate in the biosynthesis of
CC phylloquinone (vitamin K1) in plants and cyanobacteria
CC (PubMed:26023160). {ECO:0000269|PubMed:26023160,
CC ECO:0000269|PubMed:9045837}.
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, ECO:0000269|PubMed:9045837};
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 ECO:0000269|PubMed:9045837};
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, ECO:0000269|PubMed:9045837}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01813, ECO:0000269|PubMed:9045837}.
CC -!- SUBUNIT: Component of the Ubi complex metabolon, which regroups five
CC ubiquinone biosynthesis proteins (UbiE, UbiF, UbiG, UbiH and UbiI) and
CC two accessory factors (UbiK and the lipid-binding protein UbiJ).
CC {ECO:0000269|PubMed:30686758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}.
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; M87049; AAA67628.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48227.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77468.1; -; Genomic_DNA.
DR PIR; B65188; B65188.
DR RefSeq; WP_000227958.1; NZ_STEB01000021.1.
DR RefSeq; YP_026269.1; NC_000913.3.
DR AlphaFoldDB; P0A887; -.
DR SMR; P0A887; -.
DR BioGRID; 4261082; 536.
DR BioGRID; 853202; 2.
DR DIP; DIP-31831N; -.
DR IntAct; P0A887; 6.
DR STRING; 511145.b3833; -.
DR SwissLipids; SLP:000001505; -.
DR jPOST; P0A887; -.
DR PaxDb; P0A887; -.
DR PRIDE; P0A887; -.
DR EnsemblBacteria; AAT48227; AAT48227; b3833.
DR EnsemblBacteria; BAE77468; BAE77468; BAE77468.
DR GeneID; 67414381; -.
DR GeneID; 948926; -.
DR KEGG; ecj:JW5581; -.
DR KEGG; eco:b3833; -.
DR PATRIC; fig|1411691.4.peg.2875; -.
DR EchoBASE; EB1441; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_037990_0_0_6; -.
DR InParanoid; P0A887; -.
DR OMA; VRNFENL; -.
DR PhylomeDB; P0A887; -.
DR BioCyc; EcoCyc:2-OCTAPRENYL-METHOXY-BENZOQ-METH-MON; -.
DR BioCyc; MetaCyc:2-OCTAPRENYL-METHOXY-BENZOQ-METH-MON; -.
DR BRENDA; 2.1.1.163; 2026.
DR UniPathway; UPA00079; UER00169.
DR UniPathway; UPA00232; -.
DR PRO; PR:P0A887; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IDA:EcoCyc.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IMP:EcoCyc.
DR GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030580; F:quinone cofactor methyltransferase activity; IMP:EcoCyc.
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; IMP:EcoCyc.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cytoplasm; Menaquinone biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..251
FT /note="Ubiquinone/menaquinone biosynthesis C-
FT methyltransferase UbiE"
FT /id="PRO_0000193274"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT MUTAGEN 142
FT /note="G->D: In ubiE401; defective."
FT /evidence="ECO:0000269|PubMed:9045837"
SQ SEQUENCE 251 AA; 28073 MW; B1EEE209BDC68F5E CRC64;
MVDKSQETTH FGFQTVAKEQ KADMVAHVFH SVASKYDVMN DLMSFGIHRL WKRFTIDCSG
VRRGQTVLDL AGGTGDLTAK FSRLVGETGK VVLADINESM LKMGREKLRN IGVIGNVEYV
QANAEALPFP DNTFDCITIS FGLRNVTDKD KALRSMYRVL KPGGRLLVLE FSKPIIEPLS
KAYDAYSFHV LPRIGSLVAN DADSYRYLAE SIRMHPDQDT LKAMMQDAGF ESVDYYNLTA
GVVALHRGYK F
