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Items: 11

1.

deaminase

A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19 [1]. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems [1]. [1]. 21890906. Evolution of the deaminase fold and multiple origins of eukaryotic editing and mutagenic nucleic acid deaminases from bacterial toxin systems. Iyer LM, Zhang D, Rogozin IB, Aravind L;. Nucleic Acids Res. 2011; [Epub ahead of print] (from Pfam)

GO Terms:
Biological Process:
tRNA wobble adenosine to inosine editing (GO:0002100)
Molecular Function:
tRNA-specific adenosine deaminase activity (GO:0008251)
Date:
2024-10-16

Family Accession:
NF025793.5
Method:
HMM

2.

dihydrofolate reductase family protein

The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG Swiss:P25539, in combination with Pfam:PF00383, as well as in isolation in some archaebacterial proteins Swiss:P95872. This family appears to be related to Pfam:PF00186. (from Pfam)

GO Terms:
Molecular Function:
5-amino-6-(5-phosphoribosylamino)uracil reductase activity (GO:0008703)
Date:
2024-08-14

Family Accession:
NF013989.5
Method:
HMM

3.

Cytidine and deoxycytidylate deaminase zinc-binding region

Date:
2024-08-14

Family Accession:
NF012601.5
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.
new record, indexing in progress
Family Accession:
10.

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD catalyzes steps in the riboflavin biosynthesis pathway

Date:
2024-11-25

Family Accession:
10000613
Method:
Sparcle

11.

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD

This HMM describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the HMM dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model.

Gene:
ribD
GO Terms:
Molecular Function:
5-amino-6-(5-phosphoribosylamino)uracil reductase activity (GO:0008703)
Molecular Function:
diaminohydroxyphosphoribosylaminopyrimidine deaminase activity (GO:0008835)
Date:
2021-04-27

Family Accession:
TIGR00326.1
Method:
HMM

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