BACSU:FENR2

Species (Taxon ID)	Bacillus subtilis (strain 168). (224308)
Gene Name(s)	yumC
Protein Name(s)	Ferredoxin--NADP reductase 2 FNR 2 Fd-NADP(+) reductase 2
External Links
UniProt	O05268
EMBL	Z93939 AL009126
PIR	B70015
RefSeq	NP_391091.2
PDB	3LZW 3LZX
PDBsum	3LZW 3LZX
ProteinModelPortal	O05268
SMR	O05268
IntAct	O05268
MINT	MINT-8366158
STRING	224308.BSU32110
PaxDb	O05268
EnsemblBacteria	CAB15201
GeneID	936577
KEGG	bsu:BSU32110
PATRIC	18978394
GenoList	BSU32110
eggNOG	COG0492
HOGENOM	HOG000072909
InParanoid	O05268
KO	K00384
OMA	KSIVIAM
OrthoDB	EOG661H9M
PhylomeDB	O05268
BioCyc	BSUB:BSU32110-MONOMER
SABIO-RK	O05268
EvolutionaryTrace	O05268
Proteomes	UP000001570
GO	GO:0004324 GO:0050660 GO:0050661
HAMAP	MF_01685
InterPro	IPR013027 IPR022890 IPR023753 IPR001327 IPR000103
Pfam	PF00070 PF07992
PRINTS	PR00368 PR00469

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0055114	oxidation-reduction process	PMID:20878669	ECO:0000314			P		NADPH-binding domain must rotate 60° relative to the FAD-binding domain in order for hydride (movement of electrons and protons) transfer to take place as seen as figure 2d.	complete CACAO 4770
Contributes to	GO:0004324	ferredoxin-NADP+ reductase activity	PMID:20878669	ECO:0000314			F		Figure 2: Showsstructure of the BsFNR monomer in complex with NADP+ (Form I). FAD- and NAD(P)H-binding domains are shown in green and lightgreen. FAD is in yellow and NADP+ in blue. Overall structure of the BsFNR dimer in complex with NADP+.	complete
Contributes to	GO:0004324	ferredoxin-NADP+ reductase activity	PMID:20878669	ECO:0000315			F		Figure 2: Showsstructure of the BsFNR monomer in complex with NADP+ (Form I). FAD- and NAD(P)H-binding domains are shown in green and lightgreen. FAD is in yellow and NADP+ in blue. Overall structure of the BsFNR dimer in complex with NADP+.	complete
enables	GO:0004324	ferredoxin-NADP+ reductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR022890	F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023753	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR022890 InterPro:IPR023753	P		Seeded From UniProt	complete
enables	GO:0004324	ferredoxin-NADP+ reductase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.18.1.2	F		Seeded From UniProt	complete
enables	GO:0050661	NADP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000084112	F		Seeded From UniProt	complete
enables	GO:0004324	ferredoxin-NADP+ reductase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000084112	F		Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000084112	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
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References

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