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Information on EC 2.1.1.219 - tRNA (adenine57-N1/adenine58-N1)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.219
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.219 tRNA (adenine57-N1/adenine58-N1)-methyltransferase
IUBMB Comments
The enzyme catalyses the formation of N1-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs (e.g. tRNAAsp). Methyladenosine at position 57 is an obligatory intermediate for the synthesis of methylinosine, which is commonly found at position 57 of archaeal tRNAs.
The enzyme appears in viruses and cellular organisms
- 2.1.1.219
-
pyrococcus
-
avermitilis
-
t-loop
-
putidaredoxin
- s-adenosyl-l-homocysteine
-
ferredoxins
-
region-specific
Reaction Schemes
show2
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=
2
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2
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adenine57/adenine58 in tRNA
=
2
+
N1-methyladenine57/N1-methyladenine58 in tRNA
Synonyms
pabtrmi, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bi-specific tRNA adenine-N1, A57-A58-methyltransferase
bi-specific tRNA adenine-N1, A57-A58-MTase
EC 2.1.1.36
-
-
formerly, part transferred
-
PAB0283 protein
PabTrmI
PYRAB04300
TrmI
tRNA (m1A) methyltransferase
bi-specific tRNA adenine-N1, A57-A58-methyltransferase
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA = 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (adenine57/adenine58-N1)-methyltransferase
The enzyme catalyses the formation of N1-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs (e.g. tRNAAsp). Methyladenosine at position 57 is an obligatory intermediate for the synthesis of methylinosine, which is commonly found at position 57 of archaeal tRNAs.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAArg
2 S-adenosyl-L-homocysteine + adenine57/N1-methyladenine58 in tRNAArg
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Substrates: the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAArg
2 S-adenosyl-L-homocysteine + adenine57/N1-methyladenine58 in tRNAArg
Substrates: modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates only A58 in mini-tRNAArgTCT containing the G57A58A59U60 sequence
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAArg
2 S-adenosyl-L-homocysteine + adenine57/N1-methyladenine58 in tRNAArg
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates only A58 in mini-tRNAArgTCT containing the G57A58A59U60 sequence
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
Substrates: the presence of adenine at position 59 in Pyrococcus abyssi tRNA(Asp) is important for the multi-site specificity of the archaeal enzyme at both positions 57 and 58 in tRNAAsp. His78 near the active site is important for efficient catalysis
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
Substrates: modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates both A57 and A58 in mini-tRNAAsp containing the A57A58A59U60 sequence
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates both A57 and A58 in mini-tRNAAsp containing the A57A58A59U60 sequence
Products: -
Products: -
?
additional information
?
-
Substrates: methylation occurs at position 58 when position 57 contains a methylated adenine, an adenine derivative or guanine, whereas the methylation at position 57 strictly requires adenine 58 to proceed efficiently. This supports our previous conclusion that A57 is methylated before A58 in tRNAs containing the A57A58A59 sequence
Products: -
Products: -
?
additional information
?
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Substrates: methylation occurs at position 58 when position 57 contains a methylated adenine, an adenine derivative or guanine, whereas the methylation at position 57 strictly requires adenine 58 to proceed efficiently. This supports our previous conclusion that A57 is methylated before A58 in tRNAs containing the A57A58A59 sequence
Products: -
Products: -
?
additional information
?
-
Substrates: in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
Products: -
Products: -
?
additional information
?
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Substrates: construction of three oligoribonucleotide substrates of Pyrococcus abyssi TrmI containing a fluorescent 2-aminopurine at the two target positions 57 and 58, analysis of RNA binding kinetics and methylation reactions by stopped-flow and mass spectrometry, overview. PabTrmI does not modify 2-aminopurine but methylates the adjacent target adenine. 2-Aminopurine seriously impairs the methylation of A57 but not A58, confirming that PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence
Products: -
Products: -
?
additional information
?
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Substrates: construction of three oligoribonucleotide substrates of Pyrococcus abyssi TrmI containing a fluorescent 2-aminopurine at the two target positions 57 and 58, analysis of RNA binding kinetics and methylation reactions by stopped-flow and mass spectrometry, overview. PabTrmI does not modify 2-aminopurine but methylates the adjacent target adenine. 2-Aminopurine seriously impairs the methylation of A57 but not A58, confirming that PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence
Products: -
Products: -
?
additional information
?
-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: methylation occurs at position 58 when position 57 contains a methylated adenine, an adenine derivative or guanine, whereas the methylation at position 57 strictly requires adenine 58 to proceed efficiently. This supports our previous conclusion that A57 is methylated before A58 in tRNAs containing the A57A58A59 sequence
Products: -
Products: -
?
additional information
?
-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Substrates: the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: the solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA
Products: -
Products: -
?
additional information
?
-
Substrates: in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
Products: -
Products: -
?
additional information
?
-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Substrates: in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
[Comparative study of the tRNA-methylases of normal and tumor tissues. II. Positional specificity of renal and carcinoma RA methylases]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state fluorescent assay and stopped-flow kinetics with 2-aminopurine-modifed tRNA substrates, , overview
-
additional information
additional information
-
steady-state fluorescent assay and stopped-flow kinetics with 2-aminopurine-modifed tRNA substrates, , overview
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
additional information
additional information
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
additional information
-
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
additional information
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
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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). TRMI_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
282
0
32207
Swiss-Prot
-
TRMI_PYRAB
Pyrococcus abyssi (strain GE5 / Orsay)
253
0
28873
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
homotetramer
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
4 * 30000, SDS-PAGE under reducing conditions
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
concentrated by ultrafiltration, crystallisation at 20°C by the sitting-drop vapour diffusion method
crystal structure TrmI in complex with SAH is determined in two different space groups at 2.6 and 2.05 A resolution, and in complex with S-adenosyl-L-methionine (SAM) at 1.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C196S/C233S
C196S/C233S
mutant enzyme C196S/C233S is inactivated at 85°C after 20 min, wild-type enzyme is stable for more than 1 h
C196S/C233S
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
mutant enzyme C196S/C233S is inactivated at 85°C after 20 min, wild-type enzyme is stable for more than 1 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
mutant enzyme C196S/C233S is inactivated after 20 min, wild-type enzyme is stable for more than 1 h
additional information
additional information
the stabilisation of Pyrococcus abyssi TrmI at extreme temperatures involves intersubunit disulfide bridges formed between Cys196 and Cys233 that reinforce the tetrameric oligomerisation
additional information
-
the stabilisation of Pyrococcus abyssi TrmI at extreme temperatures involves intersubunit disulfide bridges formed between Cys196 and Cys233 that reinforce the tetrameric oligomerisation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme by nickel affiniyt chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roovers, M.; Wouters, J.; Bujnicki, J.M.; Tricot, C.; Stalon, V.; Grosjean, H.; Droogmans, L.
A primordial RNA modification enzyme: the case of tRNA (m1A) methyltransferase
Nucleic Acids Res.
32
465-476
2004
Pyrococcus abyssi (Q9V1J7), Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V1J7)
brenda
Guelorget, A.; Roovers, M.; Gurineau, V.; Barbey, C.; Li, X.; Golinelli-Pimpaneau, B.
Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase
Nucleic Acids Res.
38
6206-6218
2010
Pyrococcus abyssi (Q9V1J7), Pyrococcus abyssi
brenda
Hamdane, D.; Guelorget, A.; Gurineau, V.; Golinelli-Pimpaneau, B.
Dynamics of RNA modification by a multi-site-specific tRNA methyltransferase
Nucleic Acids Res.
42
11697-11706
2015
Pyrococcus abyssi (Q9V1J7), Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V1J7)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.219)
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