1FLG

CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1flgb_	All beta proteins	8-bladed beta-propeller	Quinoprotein alcohol dehydrogenase-like	Quinoprotein alcohol dehydrogenase-like	Ethanol dehydrogenase	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
A	d1flga_	All beta proteins	8-bladed beta-propeller	Quinoprotein alcohol dehydrogenase-like	Quinoprotein alcohol dehydrogenase-like	Ethanol dehydrogenase	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Quinoprotein alcohol dehydrogenase-like	8042862	3001727	SCOP2B (2022-06-29)
A	SCOP2 Family	Quinoprotein alcohol dehydrogenase-like	8030483	4002772	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Quinoprotein alcohol dehydrogenase-like	8042862	3001727	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PQQ_2	e1flgB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: PQQ_2	ECOD (1.6)
A	PQQ_2	e1flgA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: PQQ_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.140.10.10	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)
A	2.140.10.10	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13360	PQQ-like domain (PQQ_2)	PQQ-like domain	-	Repeat
A, B	PF01011	PQQ enzyme repeat (PQQ)	PQQ enzyme repeat	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (QUINOPROTEIN ETHANOL DEHYDROGENASE)	oxidoreductase activity, acting on the CH-OH group of donors, cytochrome as acceptor oxidoreductase activity alcohol dehydrogenase (cytochrome c) activity oxidoreductase activity, acting on CH-OH group of donors catalytic activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding	alcohol catabolic process catabolic process primary alcohol catabolic process organic hydroxy compound metabolic process alcohol metabolic process ethanol metabolic process organic hydroxy compound catabolic process ethanol catabolic process metabolic process cellular process small molecule metabolic process small molecule catabolic process primary alcohol metabolic process	cellular anatomical structure membrane outer membrane-bounded periplasmic space cell envelope periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat	Repeat
A, B	IPR011047	Quinoprotein alcohol dehydrogenase-like superfamily	Homologous Superfamily
A, B	IPR001479	Quinoprotein dehydrogenase, conserved site	Conserved Site
A, B	IPR017512	PQQ-dependent dehydrogenase, methanol/ethanol family	Family
A, B	IPR002372	Pyrrolo-quinoline quinone repeat	Repeat
A, B	IPR034119	PQQ-dependent type I alcohol dehydrogenase	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.