Quinoprotein amine dehydrogenase, beta chain-like
IPR011044
Definition
Quinohemoprotein amine dehydrogenase (QHNDH) from Paracoccus denitrificans is a heterotrimer consisting of alpha, beta and gamma chains PMID:11717396. The alpha chain has a four-domain structure that includes a dihaem cytochrome c, the beta chain forms a 7-bladed β-propeller that is part of the enzyme active site, and the gamma chain contains the redox factor cysteine tryptophylquinone (CTQ). The beta chain of QHNDH structurally resembles the 7-bladed β propeller of the H chain of the periplasmic quinoprotein methylamine dehydrogenase (MADH), found in methylotrophic bacteria PMID:9514722. MADH is a heterotetramer consisting of two heavy (H) chains and two light (L) chains, and contains the redox cofactor tryptophan tryptophylquinone (TTQ). There is no similarity between the quinone-containing chains of MAD and QHNDH. The β-propeller structure found in MAD and QHNDH is similar to the YVTN (Tyr-Val-Thr-Asn) repeat that folds into a β-propeller found in the N-terminal domain of archaeal surface layer proteins, which help protect cells from extreme environments PMID:12377130.
7 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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