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Information on EC 2.7.1.26 - riboflavin kinase and Organism(s) Pseudomonas aeruginosa

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EC Tree
IUBMB Comments
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates . While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase . A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP .
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Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
rfk, flavokinase, fad synthetase, riboflavin kinase, fmnat, cafads, fmn adenylyltransferase, hsrfk, atfmn/fhy, flavokinase/fad synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FK
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flavokinase
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kinase, riboflavin
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riboflavine kinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:riboflavin 5'-phosphotransferase
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9032-82-0
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0C6F617_PSEAI
312
0
34310
TrEMBL
-
A0A8B4ZF46_PSEAI
312
0
34370
TrEMBL
-
A0A8G5ITB3_PSEAI
312
0
34410
TrEMBL
-
A0A643J720_PSEAI
312
0
34368
TrEMBL
-
A0A485G8C3_PSEAI
244
0
27013
TrEMBL
-
A0A0F7QXG9_PSEAI
312
0
34340
TrEMBL
-
A0A8F9P7S0_PSEAI
312
0
34276
TrEMBL
-
A0A3M5DK05_PSEAI
93
0
10228
TrEMBL
-
A0A8G2VT83_PSEAI
312
0
34368
TrEMBL
-
A0A8G7SDJ7_PSEAI
312
0
34313
TrEMBL
-
A0A8G2UWW2_PSEAI
312
0
34358
TrEMBL
-
A0A2R3J1J4_PSEAI
312
0
34327
TrEMBL
-
A0A0A8RKR1_PSEAI
312
0
34281
TrEMBL
-
A0A8G1NK64_PSEAI
312
0
34398
TrEMBL
-
A0A5K1SES1_PSEAI
312
0
34312
TrEMBL
-
A0A8G3ZPJ3_PSEAI
312
0
34250
TrEMBL
-
A0A8F9KIP5_PSEAI
312
0
34326
TrEMBL
-