Protein Family Models for Protein (Select 489533512) - Protein Family Models

Select item 4135991.

Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase [1,2,3], but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms [4]. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite. [1]. 9501443. Purification, characterization, and mechanism of a flavin mononucleotide-dependent 2-nitropropane dioxygenase from Neurospora crassa. Gorlatova N, Tchorzewski M, Kurihara T, Soda K, Esaki N;. Appl Environ Microbiol 1998;64:1029-1033. [2]. 15582992. Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase. Francis K, Russell B, Gadda G;.. TRUNCATED at 1650 bytes (from Pfam)

GO Terms:

Molecular Function:: nitronate monooxygenase activity (GO:0018580)

Date:: 2024-10-16

Family Accession:: NF015047.5
Method:: HMM

Select item 4123932.

glutamate synthase-related protein

This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organisms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster. [1]. 8923741. Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase. Filetici P, Martegani MP, Valenzuela L, Gonzalez A, Ballario P;. Yeast 1996;12:1359-1366. (from Pfam)

GO Terms:

Biological Process:: glutamate biosynthetic process (GO:0006537)

Molecular Function:: glutamate synthase activity (GO:0015930)

Molecular Function:: oxidoreductase activity, acting on the CH-NH2 group of donors (GO:0016638)

Date:: 2024-10-16

Family Accession:: NF013784.5
Method:: HMM

Select item 4120493.

alpha-hydroxy-acid oxidizing protein

GO Terms:

Molecular Function:: oxidoreductase activity (GO:0016491)

Date:: 2024-08-14

Family Accession:: NF013253.5
Method:: HMM

Select item 4112154.

IMP dehydrogenase

This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains Pfam:PF00571 are inserted in the TIM barrel [2]. This family is a member of the common phosphate binding site TIM barrel family. [1]. 9271497. Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC;. Biochemistry 1997;36:10666-10674. [2]. 10200156. Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR;. Biochemistry 1999;38:4691-4700. (from Pfam)

GO Terms:

Molecular Function:: catalytic activity (GO:0003824)

Date:: 2024-10-16

Family Accession:: NF012690.5
Method:: HMM

Select item 3911295.