Annotations: 5KDP

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5kdpa1	Alpha and beta proteins (a/b)	PFL-like glycyl radical enzymes	PFL-like glycyl radical enzymes	automated matches	automated matches	(Oleidesulfovibrio alaskensis G20 ) [TaxId: 207559 ],	SCOPe (2.08)
A	d5kdpa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Oleidesulfovibrio alaskensis G20 ) [TaxId: 207559 ],	SCOPe (2.08)
B [auth C]	d5kdpc1	Alpha and beta proteins (a/b)	PFL-like glycyl radical enzymes	PFL-like glycyl radical enzymes	automated matches	automated matches	(Oleidesulfovibrio alaskensis G20 ) [TaxId: 207559 ],	SCOPe (2.08)
B [auth C]	d5kdpc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Oleidesulfovibrio alaskensis G20 ) [TaxId: 207559 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PFL-like glycyl radical enzymes	8087207	3001069	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	PFL-like glycyl radical enzymes	8087207	3001069	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	PFL-like	e5kdpA1	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: PFL-like	ECOD (1.6)
A	PFL-like	e5kdpA2	A: extended segments	X: Glycyl radical domain (From Topology)	H: Glycyl radical domain (From Topology)	T: Glycyl radical domain	F: PFL-like	ECOD (1.6)
B [auth C]	PFL-like	e5kdpC1	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: PFL-like	ECOD (1.6)
B [auth C]	PFL-like	e5kdpC2	A: extended segments	X: Glycyl radical domain (From Topology)	H: Glycyl radical domain (From Topology)	T: Glycyl radical domain	F: PFL-like	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)
B [auth C]	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C]	PF01228	Glycine radical (Gly_radical)	Glycine radical	-	Domain
A, B [auth C]	PF02901	Pyruvate formate lyase-like (PFL-like)	Pyruvate formate lyase-like	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C]	Choline trimethylamine-lyase	choline binding cation binding ion binding binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity lyase activity catalytic activity carbon-nitrogen lyase activity	ammonium ion metabolic process amine metabolic process catabolic process choline metabolic process metabolic process cellular process choline catabolic process biogenic amine catabolic process amine catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C]	IPR051215	Glycyl Radical Enzyme	Family
A, B [auth C]	IPR004184	Pyruvate formate lyase domain	Domain
A, B [auth C]	IPR001150	Glycine radical domain	Domain
A, B [auth C]	IPR019777	Formate C-acetyltransferase glycine radical, conserved site	Conserved Site
A, B [auth C]	IPR030897	Choline trimethylamine-lyase	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.