Protein Family Models

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase. multienzyme complex: dihydrolipoamide dehydrogenase complexed. with the binding domain of dihydrolipoamide acetyltransferase.. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

Date:

2024-04-03

This family includes Hydrogen expression/formation protein HypE Swiss:P24193, AIR synthases Swiss:P08178 EC:6.3.3.1, FGAM synthase Swiss:P35852 EC:6.3.5.3 and selenide, water dikinase Swiss:P16456 EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain [1]. [1]. 10508786. X-ray crystal structure of aminoimidazole ribonucleotide. synthetase (PurM), from the Escherichia coli purine biosynthetic. pathway at 2.5 A resolution.. Li C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE;. Structure Fold Des 1999;7:1155-1166. (from Pfam)

Date:

2024-04-03

This family includes Hydrogen expression/formation protein HypE Swiss:P24193, AIR synthases Swiss:P08178 EC:6.3.3.1, FGAM synthase Swiss:P35852 EC:6.3.5.3 and selenide, water dikinase Swiss:P16456 EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site [1]. [1]. 10508786. X-ray crystal structure of aminoimidazole ribonucleotide. synthetase (PurM), from the Escherichia coli purine biosynthetic. pathway at 2.5 A resolution.. Li C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE;. Structure Fold Des 1999;7:1155-1166. (from Pfam)

Date:

2024-04-03

selenide, water dikinase catalyzes the conversion of selenium to selenophosphate in the synthesis of SeCys-tRNA

Date:

2017-03-22

Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.

Date:

2019-09-10

In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This HMM describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring above the trusted cutoff but not aligning to the beginning of the HMM is likely have selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification, and SenB, a selenosugar-synthesizing enzyme in the pathway of selenoneine biosynthesis. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, selenoneine, SDMH, or some combination.

Gene:

selD

Date:

2022-10-11