1OYA

OLD YELLOW ENZYME AT 2 ANGSTROMS RESOLUTION: OVERALL STRUCTURE, LIGAND BINDING AND COMPARISON WITH RELATED FLAVOPROTEINS

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1oyaa_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	FMN-linked oxidoreductases	FMN-linked oxidoreductases	Old yellow enzyme (OYE)	(Saccharomyces pastorianus ) [TaxId: 27292 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	FMN-linked oxidoreductases	8058037	3000014	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00724	e1oyaA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00724	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00724	NADH:flavin oxidoreductase / NADH oxidase family (Oxidored_FMN)	NADH:flavin oxidoreductase / NADH oxidase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	OLD YELLOW ENZYME	binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pentaerythritol trinitrate reductase activity oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pentaerythritol trinitrate reductase activity oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors catalytic activity NADPH dehydrogenase activity oxidoreductase activity, acting on NAD(P)H	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR045247	Oxidoreductase Oye-like	Family
A	IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal	Domain
A	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	NADPH dehydrogenase M-CSA #319	NADPH dehydrogenase, or old yellow enzyme (OYE), isolated from Candida albicans, is a NADPH oxidoreductase. Its FMN cofactor (in plants the cofactor is FAD) is reduced by NADPH, and in turn goes on to reduce the substrate. The exact physiological substrate(s) of OYE are yet to be confirmed, though it is known to act on molecular oxygen, alpha,beta-unsaturated ketones and aldehydes, and quinones. OYE is thought to be involved in general detoxification within the cell.	Defined by 5 residues: THR:A-38 [auth A-37]HIS:A-192 [auth A-191]ASN:A-195 [auth A-194]TYR:A-197 [auth A-196]ASN:A-252 [auth A-251] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.6.99.1 (PDB Primary Data) Search M-CSA Motif + EC 1.6.99.1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.