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)
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)
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)
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)
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)
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)

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 flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	-	membrane-bounded organelle intracellular organelle cellular anatomical structure 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.