Protein Family Models

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, Gad. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

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)

Date:

2024-08-14

CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet [4]. CBS domain pairs from AMPK bind AMP or ATP [5]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [5]. Discovery and naming of the CBS domain.. [1]. 9020585. The structure of a domain common to archaebacteria and the. homocystinuria disease protein.. Bateman A;. Trends Biochem Sci 1997;22:12-13.. 3D Structure found as a sub-domain in TIM barrel of. inosine-monophosphate dehydrogenase.. [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.. Discovery of CBS domain.. [3]. 9106071. CBS domains in ClC chloride channels implicated in myotonia and. nephrolithiasis (kidney stones).. Ponting CP;. J Mol Med 1997;75:160-163.. [4]. 11524006. Regulation of human cystathionine beta-synthase by. S-adenosyl-L-methionine: evidence for two catalytically active. conformations involving an autoinhibitory domain in the. C-terminal region.. Janosik M, Kery V, . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

This HMM describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This HMM describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models.

Gene:

guaB

Date:

2024-05-29