(data stored in SCRATCH zone)

SWISSPROT: Q2IMW8_ANADE

ID   Q2IMW8_ANADE            Unreviewed;       235 AA.
AC   Q2IMW8;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE {ECO:0000256|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.163 {ECO:0000256|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.201 {ECO:0000256|HAMAP-Rule:MF_01813};
DE   AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase {ECO:0000256|HAMAP-Rule:MF_01813};
DE   AltName: Full=Demethylmenaquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_01813};
GN   Name=ubiE {ECO:0000256|HAMAP-Rule:MF_01813};
GN   OrderedLocusNames=Adeh_0374 {ECO:0000313|EMBL:ABC80150.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80150.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methyltransferase required for the conversion of
CC       demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion
CC       of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-
CC       polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
CC       {ECO:0000256|HAMAP-Rule:MF_01813}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a
CC         menaquinol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42640, Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18151, ChEBI:CHEBI:55437,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.163;
CC         Evidence={ECO:0000256|HAMAP-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-
CC         polyprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-
CC         COMP:10859, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:84166, ChEBI:CHEBI:84167;
CC         EC=2.1.1.201; Evidence={ECO:0000256|HAMAP-Rule:MF_01813};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-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
CC       methyltransferase superfamily. MenG/UbiE family.
CC       {ECO:0000256|HAMAP-Rule:MF_01813, ECO:0000256|SAAS:SAAS00572359}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01813}.
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DR   EMBL; CP000251; ABC80150.1; -; Genomic_DNA.
DR   RefSeq; WP_011419433.1; NC_007760.1.
DR   STRING; 290397.Adeh_0374; -.
DR   EnsemblBacteria; ABC80150; ABC80150; Adeh_0374.
DR   KEGG; ade:Adeh_0374; -.
DR   eggNOG; ENOG4105DDZ; Bacteria.
DR   eggNOG; COG2226; LUCA.
DR   HOGENOM; HOG000249464; -.
DR   KO; K03183; -.
DR   OMA; QKSALNC; -.
DR   BioCyc; ADEH290397:G1G5W-384-MONOMER; -.
DR   UniPathway; UPA00079; UER00169.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102955; F:S-adenosylmethionine:2-demethylmenaquinol-7 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:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR004033; UbiE/COQ5_MeTrFase.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMW8.
DR   SWISS-2DPAGE; Q2IMW8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01813,
KW   ECO:0000256|SAAS:SAAS00092033, ECO:0000313|EMBL:ABC80150.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01813,
KW   ECO:0000256|SAAS:SAAS00463460};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01813,
KW   ECO:0000256|SAAS:SAAS00463451, ECO:0000313|EMBL:ABC80150.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813}.
FT   REGION      107    108       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01813}.
FT   BINDING      66     66       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01813}.
FT   BINDING      86     86       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01813}.
SQ   SEQUENCE   235 AA;  26186 MW;  E687B31622C02000 CRC64;
     MSVNVPLPGE AHRASAVRAM FDRIAPRYDL LNRVMTLKVD QAWRRRLLSD LAPKDGERML
     DLCAGTMDVA DLARRRAPGL RVTGADFSMQ MLRRGVEKTA LPASQADAMA LPFLDARFDL
     ATVTFGMRNL ERYEVGLAEL ARVLRPGGRL GVLEFFRSES RGSRFVHGAY NRLALPVLGR
     ILSPDPEAYR YLVASMERFA SRVEFEEAAR RAGFRDVRGE TLFPGVCGLV TAVRA
//

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