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Links from Protein

Items: 14

1.

FAD synthetase

This family corresponds to the N terminal domain of the bifunctional enzyme riboflavin kinase / FAD synthetase. These enzymes have both ATP:riboflavin 5'-phospho transferase and ATP:FMN-adenylyltransferase activity [1]. They catalyse the 5'-phosphorylation of riboflavin to FMN and the adenylylation of FMN to FAD [1]. This domain is thought to have the flavin mononucleotide (FMN) adenylyltransferase activity [2]. [1]. 3023344. Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes. Manstein DJ, Pai EF;. J Biol Chem 1986;261:16169-16173. [2]. 15468322. Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima. Wang W, Kim R, Yokota H, Kim SH;. Proteins 2005;58:246-248. (from Pfam)

GO Terms:
Molecular Function:
FMN adenylyltransferase activity (GO:0003919)
Date:
2024-10-16
Family Accession:
NF018299.5
Method:
HMM
2.

riboflavin kinase

This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism [1]. This domain is thought to have kinase activity [2]. [1]. 9473052. Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC. Mack M, van Loon AP, Hohmann HP;. J Bacteriol 1998;180:950-955. [2]. 15468322. Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima. Wang W, Kim R, Yokota H, Kim SH;. Proteins 2005;58:246-248. (from Pfam)

Date:
2024-10-16
Family Accession:
NF013821.5
Method:
HMM
3.

Cytidylyltransferase-like

This family includes: Cholinephosphate cytidylyltransferase Swiss:P49585; glycerol-3-phosphate cytidylyltransferase Swiss:P27623. It also includes putative adenylyltransferases, and FAD synthases. [1]. 10208837. CTP:Phosphocholine Cytidylyltransferase: Insights into Regulatory Mechanisms and Novel Functions. Clement JM, Kent C;. Biochem Biophys Res Commun 1999;257:643-650. (from Pfam)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
biosynthetic process (GO:0009058)
Date:
2024-10-16
Family Accession:
NF013621.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.

bifunctional riboflavin kinase/FMN adenylyltransferase

bifunctional riboflavin biosynthesis protein having both ATP-riboflavin kinase and ATP-flavin mononucleotide adenylyltransferase activities

Date:
2023-03-07
Family Accession:
11481331
Method:
Sparcle
10.

bifunctional riboflavin kinase/FAD synthetase

GO Terms:
Molecular Function:
FMN adenylyltransferase activity (GO:0003919)
Date:
2021-09-01
Family Accession:
NF004162.0
Method:
HMM
11.

bifunctional riboflavin kinase/FAD synthetase

GO Terms:
Molecular Function:
FMN adenylyltransferase activity (GO:0003919)
Date:
2021-07-23
Family Accession:
NF004160.0
Method:
HMM
12.

bifunctional riboflavin kinase/FAD synthetase

Gene:
ribF
GO Terms:
Molecular Function:
FMN adenylyltransferase activity (GO:0003919)
Date:
2021-08-24
Family Accession:
NF004163.0
Method:
HMM
13.

bifunctional riboflavin kinase/FAD synthetase

Date:
2021-09-22
Family Accession:
NF004159.0
Method:
HMM
14.

riboflavin biosynthesis protein RibF

multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase).

Gene:
ribF
GO Terms:
Molecular Function:
FMN adenylyltransferase activity (GO:0003919)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
FAD biosynthetic process (GO:0006747)
Biological Process:
FMN biosynthetic process (GO:0009398)
Date:
2021-04-27
Family Accession:
TIGR00083.1
Method:
HMM
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