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InterPro: IPR019556 PQQ-dependent enzyme, C-terminal

Protein matches Help

UniProtKB

Matches:

997 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

IPR019556 PQQ-dependent_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF10535	PQQ_C	997
Signatures in BioMart

InterPro Relationships Help

Found in

IPR011047 Quinonprotein alcohol dehydrogenase-like
IPR017511 PQQ-dependent membrane bound dehydrogenase, glucose/quinate/shikimate related
IPR017512 PQQ-dependent dehydrogenase, methanol/ethanol family

Contains

IPR001479 Quinoprotein dehydrogenase, conserved site
IPR018391 Pyrrolo-quinoline quinone beta-propeller repeat

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016614 oxidoreductase activity, acting on CH-OH group of donors

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a highly conserved sequence found at the C terminus of pyrrolo-quinoline quinone (PQQ)-dependent enzymes.

Structural links Help

PDB - click here

SCOP: b.70.1.1

CATH: 2.140.10.10

Database links Help

Enzyme: EC:1.1.99

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR019556

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P12293 Methanol dehydrogenase subunit 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011047	Quinonprotein alcohol dehydrogenase-like
IPR017512	PQQ-dependent dehydrogenase, methanol/ethanol family
IPR019551	PQQ-dependent enzyme, N-terminal
IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
IPR001479	Quinoprotein dehydrogenase, conserved site
IPR019556	PQQ-dependent enzyme, C-terminal
IPR002372	Pyrrolo-quinoline quinone repeat
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

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
	Gallop PM, Paz MA, Fluckiger R, Kagan HM. PQQ, the elusive coenzyme. Trends Biochem. Sci. 14 1989 343-6 [PubMed: 2572081] http://dx.doi.org/10.1016/0968-0004(89)90169-2
	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
	He K, Nukada H, Urakami T, Murphy MP. Antioxidant and pro-oxidant properties of pyrroloquinoline quinone (PQQ): implications for its function in biological systems. Biochem. Pharmacol. 65 2003 67-74 [PubMed: 12473380] http://dx.doi.org/10.1016/S0006-2952(02)01453-3

InterPro 23.1