Annotations: 7XRM

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	F_UNCLASSIFIED	e7xrmB1	A: a/b three-layered sandwiches	X: B12-dependent dehydratase associated subunit (From Topology)	H: B12-dependent dehydratase associated subunit (From Topology)	T: B12-dependent dehydratase associated subunit	F: F_UNCLASSIFIED	ECOD (1.6)
D	F_UNCLASSIFIED	e7xrmD1	A: a/b three-layered sandwiches	X: B12-dependent dehydratase associated subunit (From Topology)	H: B12-dependent dehydratase associated subunit (From Topology)	T: B12-dependent dehydratase associated subunit	F: F_UNCLASSIFIED	ECOD (1.6)
A	F_UNCLASSIFIED	e7xrmA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e7xrmC1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: F_UNCLASSIFIED	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, D	PF05985	Ethanolamine ammonia-lyase light chain (EutC) (EutC)	Ethanolamine ammonia-lyase light chain (EutC)	-	Family
A, C	PF06751	Ethanolamine ammonia lyase large subunit (EutB) (EutB)	Ethanolamine ammonia lyase large subunit (EutB)	This family consists of several bacterial ethanolamine ammonia lyase large subunit (EutB) proteins (EC:4.3.1.7). Ethanolamine ammonia-lyase is a bacterial enzyme that catalyses the adenosylcobalamin-dependent conversion of certain vicinal amino alcoh ...	This family consists of several bacterial ethanolamine ammonia lyase large subunit (EutB) proteins (EC:4.3.1.7). Ethanolamine ammonia-lyase is a bacterial enzyme that catalyses the adenosylcobalamin-dependent conversion of certain vicinal amino alcohols to oxo compounds and ammonia. The enzyme is a heterodimer composed of subunits of Mr approximately 55,000 (EutB) and 35,000 (EutC) [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B, D	Ethanolamine ammonia-lyase small subunit	ethanolamine ammonia-lyase activity lyase activity ammonia-lyase activity catalytic activity carbon-nitrogen lyase activity vitamin binding binding cobalamin binding organic cyclic compound binding tetrapyrrole binding heterocyclic compound binding small molecule binding	ethanolamine catabolic process catabolic process alcohol catabolic process primary alcohol catabolic process ethanolamine-containing compound metabolic process organic hydroxy compound metabolic process alcohol metabolic process primary amino compound metabolic process biogenic amine catabolic process amine metabolic process primary amino compound catabolic process organic hydroxy compound catabolic process ethanolamine metabolic process metabolic process ethanolamine catabolic process catabolic process alcohol catabolic process primary alcohol catabolic process ethanolamine-containing compound metabolic process organic hydroxy compound metabolic process alcohol metabolic process primary amino compound metabolic process biogenic amine catabolic process amine metabolic process primary amino compound catabolic process organic hydroxy compound catabolic process ethanolamine metabolic process metabolic process cellular process small molecule metabolic process small molecule catabolic process biogenic amine metabolic process amine catabolic process primary alcohol metabolic process amino acid metabolic process primary metabolic process	intracellular organelle ethanolamine degradation polyhedral organelle bacterial microcompartment cellular anatomical structure intracellular anatomical structure organelle membraneless organelle intracellular membraneless organelle protein-containing complex catalytic complex ethanolamine ammonia-lyase complex intracellular protein-containing complex
A, C	Ethanolamine ammonia-lyase large subunit	ethanolamine ammonia-lyase activity lyase activity ammonia-lyase activity catalytic activity carbon-nitrogen lyase activity vitamin binding binding cobalamin binding organic cyclic compound binding tetrapyrrole binding heterocyclic compound binding small molecule binding	ethanolamine catabolic process catabolic process alcohol catabolic process primary alcohol catabolic process ethanolamine-containing compound metabolic process organic hydroxy compound metabolic process alcohol metabolic process primary amino compound metabolic process biogenic amine catabolic process amine metabolic process primary amino compound catabolic process organic hydroxy compound catabolic process ethanolamine metabolic process metabolic process ethanolamine catabolic process catabolic process alcohol catabolic process primary alcohol catabolic process ethanolamine-containing compound metabolic process organic hydroxy compound metabolic process alcohol metabolic process primary amino compound metabolic process biogenic amine catabolic process amine metabolic process primary amino compound catabolic process organic hydroxy compound catabolic process ethanolamine metabolic process metabolic process cellular process small molecule metabolic process small molecule catabolic process biogenic amine metabolic process amine catabolic process primary alcohol metabolic process amino acid metabolic process primary metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol intracellular organelle ethanolamine degradation polyhedral organelle bacterial microcompartment organelle membraneless organelle intracellular membraneless organelle protein-containing complex catalytic complex ethanolamine ammonia-lyase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, D	IPR009246	Ethanolamine ammonia-lyase small subunit	Family
B, D	IPR042251	Ethanolamine ammonia-lyase light chain, C-terminal	Homologous Superfamily
A, C	IPR044941	Ethanolamine ammonia-lyase heavy chain, N-terminal domain	Homologous Superfamily
A, C	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, C	IPR010628	Ethanolamine ammonia-lyase heavy chain	Family
A, C	IPR044939	Ethanolamine ammonia-lyase heavy chain, domain 2	Homologous Superfamily

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.