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MaoC/PaaZ C-terminal domain-containing protein
The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase [1]. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity [2]. This domain is also present in the NodN nodulation protein N. [1]. 8647101. A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. Sugino H, Sasaki M, Azakami H, Yamashita M, Murooka Y. J Bacteriol 1992;174:2485-2492. [2]. 9457873. Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae. Fukui T, Shiomi N, Doi Y;. J Bacteriol. 1998;180:667-673. (from Pfam)
aldehyde dehydrogenase family protein
This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases Swiss:P00352 EC:1.2.1.3. Succinate-semialdehyde dehydrogenase Swiss:P25526 EC:1.2.1.16. Lactaldehyde dehydrogenase Swiss:P25553 EC:1.2.1.22. Benzaldehyde dehydrogenase Swiss:P43503 EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase Swiss:Q02252 EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase Swiss:P81406 EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase Swiss:P30038 EC: 1.5.1.12. Acetaldehyde dehydrogenase Swiss:P17547 EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase Swiss:P07004 EC:1.2.1.41. This family also includes omega crystallin Swiss:P30842 an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity. [1]. 9195888. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Steinmetz CG, Xie P, Weiner H, Hurley TD;. Structure 1997;5:701-711. (from Pfam)
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
phenylacetic acid degradation bifunctional protein PaaZ
This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation [1] which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in [2]. This enzyme is related to aldehyde dehydrogenases and has domains which are members of the PF00171 and PF01575 families. This family includes paaN genes from Pseudomonas, Sinorhizobium, Rhodopseudomonas, Escherichia, Deinococcus and Corynebacterium. Another homology family (TIGR02288) includes several other species.
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