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Information on EC 1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin) and Organism(s) Pseudomonas aeruginosa

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IUBMB Comments
The enzyme, characterized from the bacterium Lactobacillus leichmannii, is similar to class II ribonucleoside-diphosphate reductase (cf. EC 1.17.4.1). However, it is specific for the triphosphate versions of its substrates. The enzyme contains an adenosylcobalamin cofactor that is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue. This radical attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6, ribonucleoside-triphosphate reductase (formate).
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Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
ribonucleotide reductase, rtpr, class ib rnr, ribonucleoside triphosphate reductase, class ii rnr, class iii rnr, class ib ribonucleotide reductase, ribonucleotide diphosphate reductase, class iii ribonucleotide reductase, class ii ribonucleotide reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase
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class II RNR
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class III RNR
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ribonucleoside triphosphate reductase
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ribonucleotide reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
2'-deoxyribonucleoside-5'-triphosphate:thioredoxin-disulfide 2'-oxidoreductase
The enzyme, characterized from the bacterium Lactobacillus leichmannii, is similar to class II ribonucleoside-diphosphate reductase (cf. EC 1.17.4.1). However, it is specific for the triphosphate versions of its substrates. The enzyme contains an adenosylcobalamin cofactor that is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue. This radical attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6, ribonucleoside-triphosphate reductase (formate).
CAS REGISTRY NUMBER
COMMENTARY hide
9068-66-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + reduced thioredoxin
dCTP + thioredoxin disulfide + H2O
show the reaction diagram
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?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
show the reaction diagram
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class III RNR
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-
?
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
show the reaction diagram
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r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
show the reaction diagram
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r
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
show the reaction diagram
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class III RNR
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-
?
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
show the reaction diagram
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r
additional information
?
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the two-component class II RNR is primarily used for DNA repair and/or possibly DNA replication at low oxygen tension. It can support bacterial growth in the absence of class I RNR activity
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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exponentialy grown cells predominantly express class I enzyme compared with class II enzyme, activity in stationary phase cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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RNRs are allosterically regulated on two levels, overall activity and substrate specificity. The substrate specificity is regulated by the binding of dNTPs to the specificity site, ATP and dATP upregulate the reduction of CDP and UDP, whereas dTTP upregulates GDP reduction and dGTP increases the rate of ADP reduction. This regulation is essential to maintain balanced dNTP pools for DNA synthesis and repairI
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A3S0ISC4_PSEAI
675
0
75934
TrEMBL
-
A0A2R3IMY0_PSEAI
675
0
75846
TrEMBL
-
A0A8G3HX02_PSEAI
675
0
76104
TrEMBL
-
A0A8F9P2I6_PSEAI
675
0
76062
TrEMBL
-
A0A8F9JUK2_PSEAI
675
0
76103
TrEMBL
-
A0A8G2UUX0_PSEAI
675
0
76122
TrEMBL
-
A0A6B1YJM0_PSEAI
675
0
76104
TrEMBL
-
A0A367MHE5_PSEAI
674
0
76033
TrEMBL
-
A0A8G6AK44_PSEAI
675
0
76062
TrEMBL
-
A0A069QHB6_PSEAI
675
0
76090
TrEMBL
-
A0A4V6DEL4_PSEAI
675
0
76117
TrEMBL
-
A0A8G7CIK7_PSEAI
675
0
76089
TrEMBL
-
A0A8G2VLY4_PSEAI
675
0
76092
TrEMBL
-
A0A8G2JUW6_PSEAI
675
0
76043
TrEMBL
-
A0A643IU58_PSEAI
675
0
76032
TrEMBL
-
A0A8G2T3K3_PSEAI
675
0
76102
TrEMBL
-
A0A8G4HII3_PSEAI
675
0
76104
TrEMBL
-
A0A8G6XEI0_PSEAI
675
0
76071
TrEMBL
-
A0A8G4H4F1_PSEAI
675
0
76104
TrEMBL
-
A0A8G3PU03_PSEAI
675
0
76089
TrEMBL
-
A0A659BAC9_PSEAI
675
0
76032
TrEMBL
-
A0A8G4I284_PSEAI
675
0
76120
TrEMBL
-
A0A8G6WHK3_PSEAI
675
0
76009
TrEMBL
-
A0A8G4DIX3_PSEAI
675
0
76029
TrEMBL
-
A0A8B5AXM0_PSEAI
675
0
76013
TrEMBL
-
A0A8G6YCT4_PSEAI
675
0
76138
TrEMBL
-
A0A8G4P308_PSEAI
675
0
76060
TrEMBL
-
A0A8G3NWU4_PSEAI
675
0
76116
TrEMBL
-
A0A225KQF9_PSEAI
675
0
76089
TrEMBL
-
A0A8G5G1K7_PSEAI
675
0
76120
TrEMBL
-
A0A8G3E8K3_PSEAI
675
0
76118
TrEMBL
-
A0A8G5UMC6_PSEAI
675
0
76109
TrEMBL
-
A0A8G7A478_PSEAI
675
0
76101
TrEMBL
-
A0A8G3J0B8_PSEAI
675
0
76148
TrEMBL
-
A0A8F9KLI3_PSEAI
675
0
76105
TrEMBL
-
A0A8G2YJN4_PSEAI
675
0
76043
TrEMBL
-
A0A8G4JAT5_PSEAI
675
0
76021
TrEMBL
-
A0A4V5LTT0_PSEAI
675
0
76103
TrEMBL
-
A0A8G4AS78_PSEAI
675
0
76134
TrEMBL
-
A0A4P0V900_PSEAI
630
0
70777
TrEMBL
-
A0A8G6HLG2_PSEAI
675
0
76089
TrEMBL
-
A0A6A9K0R2_PSEAI
675
0
76104
TrEMBL
-
A0A8G3SZQ0_PSEAI
675
0
76076
TrEMBL
-
A0A8G3DUL4_PSEAI
675
0
76120
TrEMBL
-
A0A8G2NR46_PSEAI
675
0
76042
TrEMBL
-
A0A8G6YL59_PSEAI
675
0
76119
TrEMBL
-
A0A8G7I891_PSEAI
675
0
76062
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jordan, A.; Torrents, E.; Sala, I.; Hellman, U.; Gibert, I.; Reichard, P.
Ribonucleotide reduction in Pseudomonas species: simultaneous presence of active enzymes from different classes
J. Bacteriol.
181
3974-3980
1999
Brevundimonas diminuta, Brevundimonas vesicularis, Burkholderia cepacia, Delftia acidovorans, Deinococcus radiodurans, Escherichia coli, Hydrogenophaga flava, Lactobacillus leichmannii, Paracoccus denitrificans, Mycobacterium tuberculosis, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas putida, Stenotrophomonas maltophilia, Pseudomonas stutzeri, Ralstonia pickettii, Xanthomonas campestris
Manually annotated by BRENDA team
Torrents, E.; Poplawski, A.; Sjoberg, B.M.
Two proteins mediate class II ribonucleotide reductase activity in Pseudomonas aeruginosa: expression and transcriptional analysis of the aerobic enzymes
J. Biol. Chem.
280
16571-16578
2005
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Logan, D.
Closing the circle on ribonucleotide reductases
Nat. Struct. Mol. Biol.
18
251-253
2011
Escherichia coli, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team