5NCC

Structure of Fatty acid Photodecarboxylase in complex with FAD and palmitic acid

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	GMC_oxred_C	e5nccB1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GMC_oxred_C	ECOD (1.6)
B	GMC_oxred_N	e5nccB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: GMC_oxred_N	ECOD (1.6)
C	GMC_oxred_C	e5nccC1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GMC_oxred_C	ECOD (1.6)
C	GMC_oxred_N	e5nccC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: GMC_oxred_N	ECOD (1.6)
E	GMC_oxred_C	e5nccE1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GMC_oxred_C	ECOD (1.6)
E	GMC_oxred_N	e5nccE2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: GMC_oxred_N	ECOD (1.6)
A	GMC_oxred_C	e5nccA2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GMC_oxred_C	ECOD (1.6)
A	GMC_oxred_N	e5nccA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: GMC_oxred_N	ECOD (1.6)
D	GMC_oxred_C	e5nccD2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GMC_oxred_C	ECOD (1.6)
D	GMC_oxred_N	e5nccD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: GMC_oxred_N	ECOD (1.6)
F	GMC_oxred_C	e5nccF2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: GMC_oxred_C	ECOD (1.6)
F	GMC_oxred_N	e5nccF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: GMC_oxred_N	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00732	GMC oxidoreductase (GMC_oxred_N)	GMC oxidoreductase	This family of proteins bind FAD as a cofactor.	Domain
A, B, C, D, E A, B, C, D, E, F	PF05199	GMC oxidoreductase (GMC_oxred_C)	GMC oxidoreductase	This domain found associated with Pfam:PF00732.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Fatty acid Photodecarboxylase	lyase activity catalytic activity oxidoreductase activity oxidoreductase activity, acting on CH-OH group of donors choline dehydrogenase activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	amino-acid betaine biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process amino-acid betaine metabolic process glycine betaine metabolic process glycine betaine biosynthetic process from choline ammonium ion metabolic process biosynthetic process choline metabolic process metabolic process cellular process glycine betaine biosynthetic process	cellular anatomical structure membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm intracellular membrane-bounded organelle chloroplast

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR012132	Glucose-methanol-choline oxidoreductase	Family
A, B, C, D, E A, B, C, D, E, F	IPR007867	Glucose-methanol-choline oxidoreductase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036188	FAD/NAD(P)-binding domain superfamily	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.