1E49

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant N29L/S71A

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)
A [auth P]	d1e49p_	Alpha and beta proteins (a/b)	AraD/HMP-PK domain-like	AraD/HMP-PK domain-like	AraD-like aldolase/epimerase	L-fuculose-1-phosphate aldolase	(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)
A [auth P]	SCOP2B Superfamily	AraD/HMP-PK domain-like	8032811	3001331	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 [auth P]	Aldolase_II	e1e49P1	A: a+b three layers	X: AraD-like aldolase/epimerase (From Topology)	H: AraD-like aldolase/epimerase (From Topology)	T: AraD-like aldolase/epimerase	F: Aldolase_II	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth P]	3.40.225.10	Alpha Beta	3-Layer(aba) Sandwich	L-fuculose-1-phosphate Aldolase	Class II aldolase/adducin N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth P]	PF00596	Class II Aldolase and Adducin N-terminal domain (Aldolase_II)	Class II Aldolase and Adducin N-terminal domain	This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth P]	L-FUCULOSE 1-PHOSPHATE ALDOLASE	lyase activity catalytic activity carbon-carbon lyase activity aldehyde-lyase activity L-fuculose-phosphate aldolase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	monosaccharide metabolic process arabinose metabolic process carbohydrate metabolic process catabolic process arabinose catabolic process carbohydrate catabolic process primary metabolic process D-arabinose catabolic process D-arabinose metabolic process small molecule metabolic process metabolic process cellular process pentose metabolic process monosaccharide catabolic process monosaccharide metabolic process arabinose metabolic process carbohydrate metabolic process catabolic process arabinose catabolic process carbohydrate catabolic process primary metabolic process D-arabinose catabolic process D-arabinose metabolic process small molecule metabolic process metabolic process cellular process pentose metabolic process monosaccharide catabolic process small molecule catabolic process pentose catabolic process hexose catabolic process hexose metabolic process fucose metabolic process L-fucose metabolic process fucose catabolic process L-fucose catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth P]	IPR036409	Class II aldolase/adducin N-terminal domain superfamily	Homologous Superfamily
A [auth P]	IPR004782	L-fucose phosphate aldolase	Family
A [auth P]	IPR001303	Class II aldolase/adducin N-terminal	Domain
A [auth P]	IPR050197	Aldolase class II family, sugar metabolism enzymes	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.