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InterPro: IPR011047 Quinonprotein alcohol dehydrogenase-like

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UniProtKB

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3225 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
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Accession List
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Accession

IPR011047 Quino_AlcDH-like

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.140.10.10	Quinoprotein_alc_DH-like	2359
SuperFamily	SSF50998	Quin_alc_DH_like	3208
Signatures in BioMart

InterPro Relationships Help

Children

IPR017512 PQQ-dependent dehydrogenase, methanol/ethanol family

Found in

IPR017511 PQQ-dependent membrane bound dehydrogenase, glucose/quinate/shikimate related
IPR017687 Outer membrane assembly lipoprotein YfgL

Contains

IPR001479 Quinoprotein dehydrogenase, conserved site
IPR002372 Pyrrolo-quinoline quinone repeat
IPR018391 Pyrrolo-quinoline quinone beta-propeller repeat
IPR019551 PQQ-dependent enzyme, N-terminal
IPR019556 PQQ-dependent enzyme, C-terminal

InterPro annotation

Entry Details in BioMart

Abstract

Quinoprotein alcohol dehydrogenases are a family of proteins found in methylotrophic or autotrophic bacteria. These quinoproteins use pyrroloquinoline quinone as their prosthetic group. There are three types of alcohol dehydrogenases: type I includes methanol dehydrogenase and ethanol dehydrogenase, type II includes soluble quinohaemoprotein with a C-terminal containing haem C, and type III includes quinoprotein alcohol dehydrogenase with a C-terminal cytochrome C domain [1]. These quinoproteins contain an 8-bladed beta-propeller motif, which is present in the N-terminal domain of quinoprotein alcohol dehydrogenase, ethanol dehydrogenase, and the heavy chain (alpha subunit) of methanol dehydrogenase (EC:1.1.99.8) [2, 3, 4].

Structural links Help

PDB - click here

SCOP: b.70.1.1

CATH: 2.140.10.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011047

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O75460 Serine/threonine-protein kinase/endoribonuclease IRE1

P0C2C9 F-box only protein 12

P97499 Telomerase protein component 1

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
IPR019775	WD40 repeat, conserved site
IPR010513	KEN domain, ribonuclease activator
IPR017986	WD40-repeat-containing domain
IPR017441	Protein kinase, ATP binding site
IPR017442	Serine/threonine-protein kinase-like domain
IPR001810	Cyclin-like F-box
IPR002372	Pyrrolo-quinoline quinone repeat
IPR011009	Protein kinase-like domain
IPR008850	TEP1, N-terminal
IPR000719	Protein kinase, catalytic domain
IPR013187	F-box associated type 3
IPR008858	TROVE
IPR015943	WD40/YVTN repeat-like-containing domain
IPR007111	NACHT nucleoside triphosphatase
IPR017451	F-box associated type 1
IPR019782	WD40 repeat 2
IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
IPR019781	WD40 repeat, subgroup
IPR008271	Serine/threonine-protein kinase, active site
IPR011047	Quinonprotein alcohol dehydrogenase-like
IPR011046	WD40 repeat-like-containing domain
IPR001680	WD40 repeat
	ModBase
	SWISS-MODEL
	PDB Chain

Publications Open in usermanual
1.	Anthony C. Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes. Antioxid. Redox Signal. 3 757-74 2001 [PubMed: 11761326] http://dx.doi.org/10.1089/15230860152664966
2.	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 3727-32 2002 [PubMed: 11714714] http://dx.doi.org/10.1074/jbc.M109403200
3.	Gorisch H. The ethanol oxidation system and its regulation in Pseudomonas aeruginosa. Biochim. Biophys. Acta 1647 98-102 2003 [PubMed: 12686116]
4.	Anthony C, Williams P. The structure and mechanism of methanol dehydrogenase. Biochim. Biophys. Acta 1647 18-23 2003 [PubMed: 12686102] http://dx.doi.org/10.1016/S1570-9639(03)00042-6

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

InterPro 23.1