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InterPro: IPR018391 Pyrrolo-quinoline quinone beta-propeller repeat

Protein matches Help

UniProtKB

Matches:

2525 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR018391 PQQ_beta_propeller_repeat

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
SMART	SM00564	PQQ	2525
Signatures in BioMart

InterPro Relationships Help

Children

IPR002372 Pyrrolo-quinoline quinone repeat

Found in

IPR011047 Quinonprotein alcohol dehydrogenase-like
IPR017511 PQQ-dependent membrane bound dehydrogenase, glucose/quinate/shikimate related
IPR017512 PQQ-dependent dehydrogenase, methanol/ethanol family
IPR017687 Outer membrane assembly lipoprotein YfgL
IPR019556 PQQ-dependent enzyme, C-terminal

Contains

IPR001479 Quinoprotein dehydrogenase, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

Pyrrolo-quinoline quinone (PQQ) is a redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases [1, 2]. A number of bacterial quinoproteins belong to this family.

Enzymes in this group have repeats of a beta propeller.

Structural links Help

PDB - click here

SCOP: b.70.1.1

CATH: 2.140.10.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018391

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O75460 Serine/threonine-protein kinase/endoribonuclease IRE1

O88466 Zinc finger protein 106

P32361 Serine/threonine-protein kinase/endoribonuclease IRE1

Q09499 Serine/threonine-protein kinase/endoribonuclease ire-1

Q9NIV1 Eukaryotic translation initiation factor 2-alpha kinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006567	PUG domain
IPR017986	WD40-repeat-containing domain
IPR010513	KEN domain, ribonuclease activator
IPR017441	Protein kinase, ATP binding site
IPR019782	WD40 repeat 2
IPR017442	Serine/threonine-protein kinase-like domain
IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
IPR019781	WD40 repeat, subgroup
IPR002372	Pyrrolo-quinoline quinone repeat
IPR011009	Protein kinase-like domain
IPR011047	Quinonprotein alcohol dehydrogenase-like
IPR008271	Serine/threonine-protein kinase, active site
IPR011046	WD40 repeat-like-containing domain
IPR000719	Protein kinase, catalytic domain
IPR001680	WD40 repeat
IPR015880	Zinc finger, C2H2-like
IPR007087	Zinc finger, C2H2-type
IPR015943	WD40/YVTN repeat-like-containing domain
	PDB Chain
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Duine JA, Jongejan JA. Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor. Annu. Rev. Biochem. 58 403-26 1989 [PubMed: 2549854] http://dx.doi.org/10.1146/annurev.bi.58.070189.002155
2.	Gallop PM, Paz MA, Fluckiger R, Kagan HM. PQQ, the elusive coenzyme. Trends Biochem. Sci. 14 343-6 1989 [PubMed: 2572081] http://dx.doi.org/10.1016/0968-0004(89)90169-2

Additional Reading Open in usermanual
	Nojiri M, Hira D, Yamaguchi K, Okajima T, Tanizawa K, Suzuki S. Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins. Biochemistry 45 2006 3481-92 [PubMed: 16533029] http://dx.doi.org/10.1021/bi051877j
	Williams PA, Coates L, Mohammed F, Gill R, Erskine PT, Coker A, Wood SP, Anthony C, Cooper JB. The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens. Acta Crystallogr. D Biol. Crystallogr. 61 2005 75-9 [PubMed: 15608378] http://dx.doi.org/10.1107/S0907444904026964
	Xia ZX, Dai WW, He YN, White SA, Mathews FS, Davidson VL. X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i. J. Biol. Inorg. Chem. 8 2003 843-54 [PubMed: 14505072] http://dx.doi.org/10.1007/s00775-003-0485-0
	Toyama H, Chen ZW, Fukumoto M, Adachi O, Matsushita K, Mathews FS. Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADH-IIG from Pseudomonas putida HK5. J. Mol. Biol. 352 2005 91-104 [PubMed: 16061256] http://dx.doi.org/10.1016/j.jmb.2005.06.078
	Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW. Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer. J. Biol. Chem. 277 2002 3727-32 [PubMed: 11714714] http://dx.doi.org/10.1074/jbc.M109403200

InterPro 23.1