Annotations: 5BR4

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d5br4b1	Multi-domain proteins (alpha and beta)	Dehydroquinate synthase-like	Dehydroquinate synthase-like	Iron-containing alcohol dehydrogenase	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d5br4b2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d5br4a1	Multi-domain proteins (alpha and beta)	Dehydroquinate synthase-like	Dehydroquinate synthase-like	Iron-containing alcohol dehydrogenase	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d5br4a2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Dehydroquinate synthase-like	8038927	3001905	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Dehydroquinate synthase-like	8038927	3001905	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)
B	Fe-ADH_C	e5br4B2	A: alpha bundles	X: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	H: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	T: alpha-helical domain in dehydroquinate synthase-like enzymes	F: Fe-ADH_C	ECOD (1.6)
B	Fe-ADH_N	e5br4B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Rossmann-like domain in dehydroquinate synthase-like enzymes	F: Fe-ADH_N	ECOD (1.6)
A	Fe-ADH_C	e5br4A1	A: alpha bundles	X: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	H: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	T: alpha-helical domain in dehydroquinate synthase-like enzymes	F: Fe-ADH_C	ECOD (1.6)
A	Fe-ADH_N	e5br4A2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Rossmann-like domain in dehydroquinate synthase-like enzymes	F: Fe-ADH_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	1.20.1090.10	Mainly Alpha	Up-down Bundle	Dehydroquinate synthase-like, alpha domain	Dehydroquinate synthase-like - alpha domain	CATH (4.3.0)
A	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	1.20.1090.10	Mainly Alpha	Up-down Bundle	Dehydroquinate synthase-like, alpha domain	Dehydroquinate synthase-like - alpha domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00465	Iron-containing alcohol dehydrogenase (Fe-ADH)	Iron-containing alcohol dehydrogenase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Lactaldehyde reductase	oxidoreductase activity lactaldehyde reductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors R-lactaldehyde reductase activity catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding oxidoreductase activity lactaldehyde reductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors R-lactaldehyde reductase activity catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding S-lactaldehyde reductase activity alcohol dehydrogenase [NAD(P)+] activity alcohol dehydrogenase (NAD+) activity	polyol metabolic process diol metabolic process propanediol metabolic process organic hydroxy compound metabolic process alcohol metabolic process small molecule metabolic process metabolic process cellular process glycol metabolic process diol catabolic process alcohol catabolic process catabolic process polyol catabolic process organic hydroxy compound catabolic process polyol metabolic process diol metabolic process propanediol metabolic process organic hydroxy compound metabolic process alcohol metabolic process small molecule metabolic process metabolic process cellular process glycol metabolic process diol catabolic process alcohol catabolic process catabolic process polyol catabolic process organic hydroxy compound catabolic process glycol catabolic process small molecule catabolic process monosaccharide metabolic process carbohydrate metabolic process hexose catabolic process carbohydrate catabolic process hexose metabolic process primary metabolic process fucose metabolic process L-fucose metabolic process fucose catabolic process L-fucose catabolic process monosaccharide catabolic process rhamnose catabolic process rhamnose metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001670	Alcohol dehydrogenase, iron-type/glycerol dehydrogenase GldA	Domain
A, B	IPR013460	Lactaldehyde reductase	Family
A, B	IPR039697	Iron-type alcohol dehydrogenase-like	Family
A, B	IPR018211	Alcohol dehydrogenase, iron-type, conserved site	Conserved Site

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.