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MENG_THEVB
ID   MENG_THEVB              Reviewed;         225 AA.
AC   Q8DGE4;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=2-phytyl-1,4-naphtoquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01982};
DE            EC=2.1.1.329 {ECO:0000255|HAMAP-Rule:MF_01982};
DE   AltName: Full=Demethylphylloquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01982};
GN   Name=menG {ECO:0000255|HAMAP-Rule:MF_01982}; OrderedLocusNames=tll2373;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
CC   -!- FUNCTION: Methyltransferase required for the conversion of 2-phytyl-
CC       1,4-beta-naphthoquinol to phylloquinol. {ECO:0000255|HAMAP-
CC       Rule:MF_01982}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=demethylphylloquinol + S-adenosyl-L-methionine = H(+) +
CC         phylloquinol + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:40551,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28433, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:87844; EC=2.1.1.329;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01982};
CC   -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01982}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_01982}.
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DR   EMBL; BA000039; BAC09925.1; -; Genomic_DNA.
DR   RefSeq; NP_683163.1; NC_004113.1.
DR   RefSeq; WP_011058206.1; NC_004113.1.
DR   AlphaFoldDB; Q8DGE4; -.
DR   SMR; Q8DGE4; -.
DR   STRING; 197221.22296101; -.
DR   EnsemblBacteria; BAC09925; BAC09925; BAC09925.
DR   KEGG; tel:tll2373; -.
DR   PATRIC; fig|197221.4.peg.2490; -.
DR   eggNOG; COG2226; Bacteria.
DR   OMA; WQKSALN; -.
DR   OrthoDB; 1431378at2; -.
DR   UniPathway; UPA00995; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01982; MenG_phylloquinone_subfam; 1.
DR   HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR   InterPro; IPR032904; MenG.
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.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..225
FT                   /note="2-phytyl-1,4-naphtoquinone methyltransferase"
FT                   /id="PRO_0000193340"
SQ   SEQUENCE   225 AA;  25250 MW;  E86BA421A93D2F15 CRC64;
     MTNIQALFER IAPLYDRLND QLSFGLHHVW KQMAVDWLEL PQGATALDLC CGTGDLTRLL
     ARRVGRQGRV VGLDFAAAPL AIARQRSDHY PQIEWLQGDA LAVPFAPQTF QGITIGYGLR
     NVVDIPQALR EMFRLLVPGG RAAILDFSHP QTSALEQFQQ WYLQQWVVPT ARHYGLAAEY
     DYLWPSIQAF PTPPTLCALI QQAGFERVKH YPLLGGLMAI TVAQK
 
 
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