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Database: UniProt
Entry: A0A3Q9UJU2_9ACTN
LinkDB: A0A3Q9UJU2_9ACTN
Original site: A0A3Q9UJU2_9ACTN 
ID   A0A3Q9UJU2_9ACTN        Unreviewed;       232 AA.
AC   A0A3Q9UJU2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
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_2 {ECO:0000313|EMBL:VEI03957.1};
GN   Synonyms=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN   ORFNames=C0Z10_02730 {ECO:0000313|EMBL:AZZ38839.1}, FEZ32_07630
GN   {ECO:0000313|EMBL:QCV88242.1}, NCTC13652_02175
GN   {ECO:0000313|EMBL:VEI03957.1};
OS   Acidipropionibacterium jensenii.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Acidipropionibacterium.
OX   NCBI_TaxID=1749 {ECO:0000313|EMBL:AZZ38839.1, ECO:0000313|Proteomes:UP000285875};
RN   [1] {ECO:0000313|Proteomes:UP000285875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS280 {ECO:0000313|Proteomes:UP000285875};
RA   Deptula P., Laine P., Smolander O.-P., Paulin L., Auvinen P., Varmanen P.;
RT   "Whole genome sequencing of Acidipropionibacterium jensenii strains JS279
RT   and JS280.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VEI03957.1, ECO:0000313|Proteomes:UP000277858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13652 {ECO:0000313|EMBL:VEI03957.1,
RC   ECO:0000313|Proteomes:UP000277858};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AZZ38839.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JS280 {ECO:0000313|EMBL:AZZ38839.1};
RX   PubMed=31671651;
RA   Deptula P., Loivamaa I., Smolander O.P., Laine P., Roberts R.J.,
RA   Piironen V., Paulin L., Savijoki K., Auvinen P., Varmanen P.;
RT   "Red-Brown Pigmentation of Acidipropionibacterium jensenii Is Tied to
RT   Haemolytic Activity and cyl-Like Gene Cluster.";
RL   Microorganisms 7:0-E512(2019).
RN   [4] {ECO:0000313|EMBL:QCV88242.1, ECO:0000313|Proteomes:UP000310120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAM 19038 {ECO:0000313|EMBL:QCV88242.1,
RC   ECO:0000313|Proteomes:UP000310120};
RA   Roder T., Wuthrich D., Sattari Z., von Ah U., Bar C., Ronchi F.,
RA   Macpherson A.J., Ganal-Vonarburg S.C., Bruggmann R., Vergeres G.;
RT   "The metagenome of a microbial culture collection derived from dairy
RT   environment covers the genomic content of the human microbiome.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP025570; AZZ38839.1; -; Genomic_DNA.
DR   EMBL; CP040635; QCV88242.1; -; Genomic_DNA.
DR   EMBL; LR134473; VEI03957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9UJU2; -.
DR   STRING; 1122997.GCA_000425285_00939; -.
DR   KEGG; aji:C0Z10_02730; -.
DR   OrthoDB; 9808140at2; -.
DR   UniPathway; UPA00079; UER00169.
DR   Proteomes; UP000277858; Chromosome 1.
DR   Proteomes; UP000285875; Chromosome.
DR   Proteomes; UP000310120; Chromosome.
DR   GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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   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:SF24; 2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43591; METHYLTRANSFERASE; 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; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
KW   Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW   Rule:MF_01813};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01813}; Reference proteome {ECO:0000313|Proteomes:UP000277858};
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}; Ubiquinone {ECO:0000313|EMBL:VEI03957.1}.
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         104..105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ   SEQUENCE   232 AA;  25370 MW;  6BF77B594D2961CD CRC64;
     MLTTRATLDK HHSDVASMFD GVAQRYDLMN SIMTMGAVDH WRELVVEAVE PQPGQTILDL
     AAGTGTSSAT FAAHGAQVYP TDISMGMLQV GHQRQPDLHF VGGDATRLPY ADDVFDAVTI
     SYGLRNVEDT SAALSEMLRV TRPGGRIVVC EFSTPTWAPF RHLYRDYLLS AIPAMARLAS
     SNQDAYDYLA ESILAWPDQA ALADLMARAG WQAVAWRNIC GGVVSLHRAW KA
//
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