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InterPro: IPR002364 Quinone oxidoreductase/zeta-crystallin, conserved site

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1988 proteins

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Accession List
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Accession

IPR002364 Quin_OxRdtase/zeta-crystal_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01162	QOR_ZETA_CRYSTAL	1988
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002085 Alcohol dehydrogenase superfamily, zinc-containing
IPR013149 Alcohol dehydrogenase, zinc-binding
IPR014182 Alcohol dehydrogenase, zinc-binding type 1
IPR016040 NAD(P)-binding domain

GO Term annotation Help

Function

GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

NADP-dependent quinone oxidoreductases (EC:1.6.5.5) are part of the zinc-containing alcohol dehydrogenase family of enzymes.

The NADP-dependent quinone oxidoreductase (EC:1.6.5.5) is found in bacteria (gene qor), in yeast and in mammals where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin [1]. The sequence of quinone oxidoreductase is distantly related to that other zinc-containing alcohol dehydrogenases and it lacks the zinc-ligand residues. The Torpedo fish and mammalian synaptic vesicle membrane protein vat-1 is related to qor.

Structural links Help

PDB - click here

SCOP: c.2.1.1

CATH: 3.40.50.720

Database links Help

PDBe-motif: PS01162

PROSITE doc: PDOC00058

Blocks: IPB002364

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002364

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P28304 Quinone oxidoreductase

P38230 Probable quinone oxidoreductase

P47199 Quinone oxidoreductase

Q08257 Quinone oxidoreductase

Q9ZUC1 Quinone oxidoreductase-like protein At1g23740, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002364	Quinone oxidoreductase/zeta-crystallin, conserved site
IPR013149	Alcohol dehydrogenase, zinc-binding
IPR013154	Alcohol dehydrogenase GroES-like
IPR011032	GroES-like
IPR016040	NAD(P)-binding domain
IPR002085	Alcohol dehydrogenase superfamily, zinc-containing
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Jornvall H, Persson B, Du Bois GC, Lavers GC, Chen JH, Gonzalez P, Rao PV, Zigler JS Jr. Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic. FEBS Lett. 322 240-4 1993 [PubMed: 8486156] http://dx.doi.org/10.1016/0014-5793(93)81578-N

Additional Reading Open in usermanual
	Sun HW, Plapp BV. Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family. J. Mol. Evol. 34 1992 522-35 [PubMed: 1593644] http://dx.doi.org/10.1007/BF00160465
	Koga H, Aramaki H, Yamaguchi E, Takeuchi K, Horiuchi T, Gunsalus IC. camR, a negative regulator locus of the cytochrome P-450cam hydroxylase operon. J. Bacteriol. 166 1986 1089-95 [PubMed: 3011733] http://jb.asm.org/cgi/content/abstract/166/3/1089
	Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ. Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J. Mol. Biol. 249 1995 785-99 [PubMed: 7602590] http://dx.doi.org/10.1006/jmbi.1995.0337
	Persson B, Hallborn J, Walfridsson M, Hahn-Hagerdal B, Keranen S, Penttila M, Jornvall H. Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types. FEBS Lett. 324 1993 9-14 [PubMed: 8504864] http://dx.doi.org/10.1016/0014-5793(93)81522-2
	Knight ME, Halpin C, Schuch W. Identification and characterisation of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco. Plant Mol. Biol. 19 1992 793-801 [PubMed: 1643282] http://dx.doi.org/10.1007/BF00027075

InterPro 23.1