EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR002372 Pyrrolo-quinoline quinone repeat

Protein matches Help

UniProtKB

Matches:

2028 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

IPR002372 PQQ_repeat

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01011	PQQ	2028
Signatures in BioMart

InterPro Relationships Help

Parent

IPR018391 Pyrrolo-quinoline quinone beta-propeller 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

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

Database links Help

PANDIT: PF01011

Blocks: IPB002372

COMe: PRX000474

Pfam Clan: CL0186.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002372

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O75460 Serine/threonine-protein kinase/endoribonuclease IRE1

P12293 Methanol dehydrogenase subunit 1

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

Q80WC9 Acyl-CoA synthetase family member 4

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
IPR017512	PQQ-dependent dehydrogenase, methanol/ethanol family
IPR019551	PQQ-dependent enzyme, N-terminal
IPR010513	KEN domain, ribonuclease activator
IPR017441	Protein kinase, ATP binding site
IPR017442	Serine/threonine-protein kinase-like domain
IPR001479	Quinoprotein dehydrogenase, conserved site
IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
IPR020845	AMP-binding, conserved site
IPR019556	PQQ-dependent enzyme, C-terminal
IPR002372	Pyrrolo-quinoline quinone repeat
IPR011009	Protein kinase-like domain
IPR011047	Quinonprotein alcohol dehydrogenase-like
IPR008271	Serine/threonine-protein kinase, active site
IPR000719	Protein kinase, catalytic domain
IPR006162	Phosphopantetheine attachment site
IPR009081	Acyl carrier protein-like
IPR000873	AMP-dependent synthetase/ligase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

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 Z, Dai W, Zhang Y, White SA, Boyd GD, Mathews FS. Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1. J. Mol. Biol. 259 1996 480-501 [PubMed: 8676383] http://dx.doi.org/10.1006/jmbi.1996.0334
	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
	Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C. The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A. Structure 3 1995 177-87 [PubMed: 7735834] http://dx.doi.org/10.1016/S0969-2126(01)00148-4

InterPro 23.1