(data stored in SCRATCH zone)

SWISSPROT: D7A210_STAND

ID   D7A210_STAND            Unreviewed;       262 AA.
AC   D7A210;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
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=Snov_0292 {ECO:0000313|EMBL:ADH87626.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87626.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87626.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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; CP002026; ADH87626.1; -; Genomic_DNA.
DR   RefSeq; WP_013165131.1; NC_014217.1.
DR   STRING; 639283.Snov_0292; -.
DR   EnsemblBacteria; ADH87626; ADH87626; Snov_0292.
DR   KEGG; sno:Snov_0292; -.
DR   eggNOG; ENOG4105DDZ; Bacteria.
DR   eggNOG; COG2226; LUCA.
DR   HOGENOM; HOG000249463; -.
DR   KO; K03183; -.
DR   OMA; VRNFENL; -.
DR   OrthoDB; 1431378at2; -.
DR   BioCyc; SNOV639283:G1GLM-296-MONOMER; -.
DR   UniPathway; UPA00079; UER00169.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000006633; 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   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.
PE   3: Inferred from homology;
DR   PRODOM; D7A210.
DR   SWISS-2DPAGE; D7A210.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
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:ADH87626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
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:ADH87626.1};
KW   Ubiquinone {ECO:0000313|EMBL:ADH87626.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813}.
FT   REGION      134    135       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01813}.
FT   BINDING      85     85       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01813}.
FT   BINDING     106    106       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01813}.
SQ   SEQUENCE   262 AA;  28545 MW;  43333D9500A98C61 CRC64;
     MAADTRTDGT TSEAADTHFG FRTVPLGEKQ RMVDEVFHSV ARRYDLMNDL MSLGLHRAWK
     DLLVSRLRPP KTDRSFRLLD VAGGTGDVSF RTVEAGGAGT SATVADINGG MLGVGRERAA
     SLGLSDRVEF VEANAEELPF ADKSFDATTI AFGIRNVPRM DKALAEMRRV LKPGGRCFVL
     EFSRVDVPGL DAIYDAYSFK LIPPMGKLVT GDAESYQYLV ESIRKFPSPE AFAEMMRAAG
     FSRVDVTPLT GGIVCLHSGV RI
//

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