Any feedback?
No. of entries
Information on EC 2.1.1.400 - 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol 3-C-methyltransferase
for references in articles please use BRENDA:EC2.1.1.400
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.400 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol 3-C-methyltransferase
IUBMB Comments
The enzyme, characterized from the archaeon Methanococcus maripaludis, participates in the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor of EC 1.12.98.2, 5,10-methenyltetrahydromethanopterin hydrogenase (also known as [Fe]-hydrogenase).
The expected taxonomic range for this enzyme is: Methanomada group
Reaction Schemes
show+
=
+
+
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
=
+
6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Synonyms
hcgC, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hcgC
hcgC
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol = S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol 3-C-methyltransferase
The enzyme, characterized from the archaeon Methanococcus maripaludis, participates in the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor of EC 1.12.98.2, 5,10-methenyltetrahydromethanopterin hydrogenase (also known as [Fe]-hydrogenase).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Methanococcus maripaludis DSM 14266
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Methanococcus maripaludis DSM 14266
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Methanococcus maripaludis DSM 14266
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
Methanococcus maripaludis DSM 14266
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme Y51F, pH and temperature not specified in the publication
-
7.3
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
wild type enzyme, pH and temperature not specified in the publication
-
7.6
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme S175A, pH and temperature not specified in the publication
-
36
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme S233A, pH and temperature not specified in the publication
-
100
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme T6V, pH and temperature not specified in the publication
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0042
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme Y51F, pH and temperature not specified in the publication
-
0.0053
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme T6V, pH and temperature not specified in the publication
-
0.0057
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme S233A, pH and temperature not specified in the publication
-
0.022
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme S175A, pH and temperature not specified in the publication
-
0.04
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
wild type enzyme, pH and temperature not specified in the publication
-
0.042
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
-
pH and temperature not specified in the publication
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000053
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme T6V, pH and temperature not specified in the publication
-
0.000157
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme S233A, pH and temperature not specified in the publication
-
0.00077
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme Y51F, pH and temperature not specified in the publication
-
0.0028
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
mutant enzyme S175A, pH and temperature not specified in the publication
-
0.0055
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
wild type enzyme, pH and temperature not specified in the publication
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Methanococcus maripaludis DSM 14266
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the enzyme is involved in iron-guanylylpyridinol biosynthesis
metabolism
-
the enzyme participates in [Fe]-Hydrogenase cofactor biosynthesis
metabolism
Methanococcus maripaludis DSM 14266
-
the enzyme is involved in iron-guanylylpyridinol biosynthesis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q6LX54_METMP
Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
260
0
29262
TrEMBL
-
Q6LX55_METMP
Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
159
0
17189
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with S-adenosyl-L-homocysteine and substrate 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E209Q
the mutant shows severely reduced activity compared to the wild type enzyme
S175A
the mutant shows reduced activity compared to the wild type enzyme
S233A
the mutant shows reduced activity compared to the wild type enzyme
T179V
the mutant shows severely reduced activity compared to the wild type enzyme
T6V
the mutant shows reduced activity compared to the wild type enzyme
Y51F
the mutant shows reduced activity compared to the wild type enzyme
S175A
Methanococcus maripaludis DSM 14266
-
the mutant shows reduced activity compared to the wild type enzyme
-
S233A
Methanococcus maripaludis DSM 14266
-
the mutant shows reduced activity compared to the wild type enzyme
-
T179V
Methanococcus maripaludis DSM 14266
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
T6V
Methanococcus maripaludis DSM 14266
-
the mutant shows reduced activity compared to the wild type enzyme
-
Y51F
Methanococcus maripaludis DSM 14266
-
the mutant shows reduced activity compared to the wild type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Ni-NTA column chromatography, and Superdex 200 gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujishiro, T.; Bai, L.; Xu, T.; Xie, X.; Schick, M.; Kahnt, J.; Rother, M.; Hu, X.; Ermler, U.; Shima, S.
Identification of HcgC as a SAM-dependent pyridinol methyltransferase in [Fe]-hydrogenase cofactor biosynthesis
Angew. Chem. Int. Ed. Engl.
55
9648-9651
2016
Methanocaldococcus jannaschii
brenda
Bai, L.; Wagner, T.; Xu, T.; Hu, X.; Ermler, U.; Shima, S.
A water-bridged H-bonding network contributes to the catalysis of the SAM-dependent C-methyltransferase HcgC
Angew. Chem. Int. Ed. Engl.
56
10806-10809
2017
Methanococcus maripaludis (Q6LX54), Methanococcus maripaludis DSM 14266 (Q6LX54)
brenda
Schaupp, S.; Arriaza-Gallardo, F.J.; Pan, H.J.; Kahnt, J.; Angelidou, G.; Paczia, N.; Costa, K.; Hu, X.; Shima, S.
In vitro biosynthesis of the [Fe]-hydrogenase cofactor verifies the proposed biosynthetic precursors
Angew. Chem. Int. Ed. Engl.
61
e202200994
2022
Methanococcus maripaludis
brenda
Arriaza-Gallardo, F.J.; Zheng, Y.C.; Gehl, M.; Nomura, S.; Fernandes-Queiroz, J.P.; Shima, S.
[Fe]-hydrogenase, cofactor biosynthesis and engineering
Chembiochem
24
e202300330
2023
Methanococcus maripaludis (Q6LX54)
brenda
Bai, L.; Fujishiro, T.; Huang, G.; Koch, J.; Takabayashi, A.; Yokono, M.; Tanaka, A.; Xu, T.; Hu, X.; Ermler, U.; Shima, S.
Towards artificial methanogenesis biosynthesis of the [Fe]-hydrogenase cofactor and characterization of the semi-synthetic hydrogenase
Faraday Discuss.
198
37-58
2017
Methanococcus maripaludis (Q6LX55), Methanococcus maripaludis DSM 14266 (Q6LX55), Methanothermobacter marburgensis
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.400)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
