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InterPro: IPR011044 Quinoprotein amine dehydrogenase, beta chain-like

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3531 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR011044 Quino_amine_DH_bsu

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SuperFamily	SSF50969	Amine_DH_B_like	3531
Signatures in BioMart

InterPro Relationships Help

Found in

IPR008311 Uncharacterised conserved protein UCP028101
IPR009451 Methylamine dehydrogenase heavy subunit
IPR013476 Methylamine dehydrogenase heavy chain
IPR014167 Tol-Pal system beta propeller repeat-containing protein, TolB
IPR015943 WD40/YVTN repeat-like-containing domain

InterPro annotation

Entry Details in BioMart

Abstract

Quinohemoprotein amine dehydrogenase (QHNDH) from Paracoccus denitrificans is a heterotrimer consisting of alpha, beta and gamma chains [1]. The alpha chain has a four-domain structure that includes a dihaem cytochrome c, the beta chain forms a 7-bladed beta-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 beta propeller of the H chain of the periplasmic quinoprotein methylamine dehydrogenase (MADH), found in methylotrophic bacteria [2]. 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 beta-propeller structure found in MAD and QHNDH is similar to the YVTN (Tyr-Val-Thr-Asn) repeat that folds into a beta-propeller found in the N-terminal domain of archaeal surface layer proteins, which help protect cells from extreme environments [3].

Structural links Help

PDB - click here

SCOP: b.68.4.1 , b.69.2.1 , b.69.2.2 , c.51.2.1

CATH: 2.120.10.30 , 2.130.10.10 , 3.40.50.10070

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011044

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2AHJ4 Bromodomain and WD repeat-containing protein 3

A6ZU71 Ribosome biogenesis protein NSA1

B1ANS9 WD repeat-containing protein 64

P34609 JNK-interacting protein

Q9SJT9 Coatomer subunit alpha-2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010714	Coatomer, alpha subunit, C-terminal
IPR019775	WD40 repeat, conserved site
IPR017986	WD40-repeat-containing domain
IPR019782	WD40 repeat 2
IPR019781	WD40 repeat, subgroup
IPR019143	JNK/Rab-associated protein-1
IPR011044	Quinoprotein amine dehydrogenase, beta chain-like
IPR001487	Bromodomain
IPR006692	Coatomer, WD associated region
IPR011046	WD40 repeat-like-containing domain
IPR001680	WD40 repeat
IPR020472	G-protein beta WD-40 repeat, region
IPR015943	WD40/YVTN repeat-like-containing domain
IPR016391	Coatomer, alpha subunit
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Datta S, Mori Y, Takagi K, Kawaguchi K, Chen ZW, Okajima T, Kuroda S, Ikeda T, Kano K, Tanizawa K, Mathews FS. Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking. Proc. Natl. Acad. Sci. U.S.A. 98 14268-73 2001 [PubMed: 11717396] http://dx.doi.org/10.1073/pnas.241429098
2.	Chen L, Doi M, Durley RC, Chistoserdov AY, Lidstrom ME, Davidson VL, Mathews FS. Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution. J. Mol. Biol. 276 131-49 1998 [PubMed: 9514722] http://dx.doi.org/10.1006/jmbi.1997.1511
3.	Jing H, Takagi J, Liu JH, Lindgren S, Zhang RG, Joachimiak A, Wang JH, Springer TA. Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins. Structure 10 1453-64 2002 [PubMed: 12377130] http://dx.doi.org/10.1016/S0969-2126(02)00840-7

Additional Reading Open in usermanual
	Sun D, Chen ZW, Mathews FS, Davidson VL. Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin. Biochemistry 41 2002 13926-33 [PubMed: 12437349] http://dx.doi.org/10.1021/bi026654x
	Datta S, Ikeda T, Kano K, Mathews FS. Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution. Acta Crystallogr. D Biol. Crystallogr. 59 2003 1551-6 [PubMed: 12925784] http://dx.doi.org/10.1107/S090744490301429X
	Loftus SR, Walker D, Mate MJ, Bonsor DA, James R, Moore GR, Kleanthous C. Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. Proc. Natl. Acad. Sci. U.S.A. 103 2006 12353-8 [PubMed: 16894158] http://dx.doi.org/10.1073/pnas.0603433103
	Bonsor DA, Grishkovskaya I, Dodson EJ, Kleanthous C. Molecular mimicry enables competitive recruitment by a natively disordered protein. J. Am. Chem. Soc. 129 2007 4800-7 [PubMed: 17375930] http://dx.doi.org/10.1021/ja070153n
	Satoh A, Kim JK, Miyahara I, Devreese B, Vandenberghe I, Hacisalihoglu A, Okajima T, Kuroda S, Adachi O, Duine JA, Van Beeumen J, Tanizawa K, Hirotsu K. Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges. J. Biol. Chem. 277 2002 2830-4 [PubMed: 11704672] http://dx.doi.org/10.1074/jbc.M109090200

InterPro 24.0