1OGY

Crystal structure of the heterodimeric nitrate reductase from Rhodobacter sphaeroides

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ogya1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
A	d1ogya2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
E	d1ogye1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
E	d1ogye2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
G	d1ogyg1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
G	d1ogyg2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
I	d1ogyi1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
I	d1ogyi2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
M	d1ogym1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
M	d1ogym2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
C	d1ogyc1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
C	d1ogyc2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
K	d1ogyk1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
K	d1ogyk2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
O	d1ogyo1	All beta proteins	Double psi beta-barrel	ADC-like	Formate dehydrogenase/DMSO reductase, C-terminal domain	Periplasmic nitrate reductase alpha chain, NapA	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
O	d1ogyo2	Alpha and beta proteins (a/b)	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Formate dehydrogenase/DMSO reductase, domains 1-3	Periplasmic nitrate reductase alpha chain	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
B	d1ogyb_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
D	d1ogyd_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
F	d1ogyf_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
J	d1ogyj_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
L	d1ogyl_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
N	d1ogyn_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
P	d1ogyp_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)
H	d1ogyh_	All alpha proteins	Multiheme cytochromes	Multiheme cytochromes	Di-heme elbow motif	Periplasmic nitrate reductase subunit NapB	(Cereibacter sphaeroides ) [TaxId: 1063 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Formate dehydrogenase/DMSO reductase domains 1-3	8025121	4000801	SCOP2 (2022-06-29)
A	SCOP2 Family	Formate dehydrogenase/DMSO reductase C-terminal domain	8025120	4002360	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ADC-like	8037499	3001132	SCOP2 (2022-06-29)
E	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	ADC-like	8037499	3001132	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	Formate dehydrogenase/DMSO reductase domains 1-3	8037500	3001453	SCOP2B (2022-06-29)
B	SCOP2 Family	NapB-like	8089677	4000355	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Di-heme elbow motif	8089678	3000145	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	Molydop_binding	e1ogyA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
A	Molybdop_Fe4S4	e1ogyA3	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
A	Molybdopterin_2nd	e1ogyA5	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
A	Molybdopterin_1st_1	e1ogyA4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
E	Molydop_binding	e1ogyE1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
E	Molybdop_Fe4S4	e1ogyE4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
E	Molybdopterin_2nd	e1ogyE2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
E	Molybdopterin_1st_1	e1ogyE3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
G	Molydop_binding	e1ogyG1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
G	Molybdop_Fe4S4	e1ogyG4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
G	Molybdopterin_2nd	e1ogyG2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
G	Molybdopterin_1st_1	e1ogyG3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
I	Molydop_binding	e1ogyI1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
I	Molybdop_Fe4S4	e1ogyI4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
I	Molybdopterin_2nd	e1ogyI2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
I	Molybdopterin_1st_1	e1ogyI3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
M	Molydop_binding	e1ogyM1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
M	Molybdop_Fe4S4	e1ogyM4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
M	Molybdopterin_2nd	e1ogyM2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
M	Molybdopterin_1st_1	e1ogyM3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
C	Molydop_binding	e1ogyC1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
C	Molybdop_Fe4S4	e1ogyC4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
C	Molybdopterin_2nd	e1ogyC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
C	Molybdopterin_1st_1	e1ogyC3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
K	Molydop_binding	e1ogyK1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
K	Molybdop_Fe4S4	e1ogyK4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
K	Molybdopterin_2nd	e1ogyK2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
K	Molybdopterin_1st_1	e1ogyK3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
O	Molydop_binding	e1ogyO1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: double psi	F: Molydop_binding	ECOD (1.6)
O	Molybdop_Fe4S4	e1ogyO4	A: a+b two layers	X: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domain 1	F: Molybdop_Fe4S4	ECOD (1.6)
O	Molybdopterin_2nd	e1ogyO2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_2nd	ECOD (1.6)
O	Molybdopterin_1st_1	e1ogyO3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)	T: Formate dehydrogenase/DMSO reductase, domains 2 and 3	F: Molybdopterin_1st_1	ECOD (1.6)
B	NapB	e1ogyB1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
D	NapB	e1ogyD1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
F	NapB	e1ogyF1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
J	NapB	e1ogyJ1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
L	NapB	e1ogyL1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
N	NapB	e1ogyN1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
P	NapB	e1ogyP1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)
H	NapB	e1ogyH1	A: few secondary structure elements	X: Multiheme cytochromes	H: Di-heme elbow motif (From Topology)	T: Di-heme elbow motif	F: NapB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
A	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
A	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
E	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
E	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
E	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
G	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
G	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
G	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
G	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
I	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
I	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
I	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
I	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
M	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
M	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
M	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
M	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
C	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
C	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
C	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
K	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
K	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
K	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
K	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)
O	3.30.200.210	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
O	3.40.50.740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
O	3.40.228.10	Alpha Beta	3-Layer(aba) Sandwich	Dimethylsulfoxide Reductase	domain 2	CATH (4.3.0)
O	2.40.40.20	Mainly Beta	Beta Barrel	Barwin-like endoglucanases		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C, E, G, I A, C, E, G, I, K, M, O	PF01568	Molydopterin dinucleotide binding domain (Molydop_binding)	Molydopterin dinucleotide binding domain	This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entir ...	This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2].	Domain
A, C, E, G, I A, C, E, G, I, K, M, O	PF04879	Molybdopterin oxidoreductase Fe4S4 domain (Molybdop_Fe4S4)	Molybdopterin oxidoreductase Fe4S4 domain	This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface [1].	Domain
A, C, E, G, I A, C, E, G, I, K, M, O	PF00384	Molybdopterin oxidoreductase (Molybdopterin)	Molybdopterin oxidoreductase	-	Family
B, D, F, H, J B, D, F, H, J, L, N, P	PF03892	Nitrate reductase cytochrome c-type subunit (NapB) (NapB)	Nitrate reductase cytochrome c-type subunit (NapB)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C, E, G, I A, C, E, G, I, K, M, O	PERIPLASMIC NITRATE REDUCTASE	cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding nitrate reductase activity oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors catalytic activity molybdenum ion binding nitrate reductase (cytochrome) activity oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding nitrate reductase activity oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors catalytic activity molybdenum ion binding nitrate reductase (cytochrome) activity oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor oxidoreductase activity, acting on a heme group of donors organic cyclic compound binding molybdopterin cofactor binding iron-sulfur cluster binding 4 iron, 4 sulfur cluster binding metal cluster binding electron transfer activity	nitrate assimilation oxoacid metabolic process cellular metabolic process organic acid metabolic process reactive nitrogen species metabolic process nitrogen cycle metabolic process organic substance metabolic process metabolic process small molecule metabolic process cellular process nitrate metabolic process cellular respiration energy derivation by oxidation of organic compounds generation of precursor metabolites and energy nitrate assimilation oxoacid metabolic process cellular metabolic process organic acid metabolic process reactive nitrogen species metabolic process nitrogen cycle metabolic process organic substance metabolic process metabolic process small molecule metabolic process cellular process nitrate metabolic process cellular respiration energy derivation by oxidation of organic compounds generation of precursor metabolites and energy organonitrogen compound metabolic process Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process organonitrogen compound biosynthetic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process organic cyclic compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process organic cyclic compound biosynthetic process phosphate-containing compound metabolic process organic substance biosynthetic process protein metabolic process macromolecule metabolic process phosphorus metabolic process	protein-containing complex catalytic complex oxidoreductase complex periplasmic space cellular anatomical entity
B, D, F, H, J B, D, F, H, J, L, N, P	DIHEME CYTOCHROME C NAPB MOLECULE: NITRATE REDUCTASE	cation binding ion binding binding metal ion binding small molecule binding	cellular respiration energy derivation by oxidation of organic compounds cellular metabolic process metabolic process cellular process generation of precursor metabolites and energy anaerobic respiration	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C, E, G, I A, C, E, G, I, K, M, O	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain	Domain
A, C, E, G, I A, C, E, G, I, K, M, O	IPR006657	Molybdopterin dinucleotide-binding domain	Domain
A, C, E, G, I A, C, E, G, I, K, M, O	IPR006656	Molybdopterin oxidoreductase	Domain
A, C, E, G, I A, C, E, G, I, K, M, O	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, C, E, G, I A, C, E, G, I, K, M, O	IPR009010	Aspartate decarboxylase-like domain superfamily	Homologous Superfamily
A, C, E, G, I A, C, E, G, I, K, M, O	IPR010051	Periplasmic nitrate reductase, large subunit	Family
A, C, E, G, I A, C, E, G, I, K, M, O	IPR041957	Nitrate reductase NapA-like, molybdopterin-binding domain	Domain
A, C, E, G, I A, C, E, G, I, K, M, O	IPR027467	Molybdopterin oxidoreductase, molybdopterin cofactor binding site	Binding Site
A, C, E, G, I A, C, E, G, I, K, M, O	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal	Conserved Site
B, D, F, H, J B, D, F, H, J, L, N, P	IPR036280	Multiheme cytochrome superfamily	Homologous Superfamily
B, D, F, H, J B, D, F, H, J, L, N, P	IPR005591	Nitrate reductase cytochrome c-type subunit NapB	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
E	nitrate reductase M-CSA #276	Nitrate reductase is a molybdenum-bis(molybdopterin guanine dinucleotide) dependent enzyme. It catalyses the reduction of nitrate to nitrite and water. The protein associates with NapB, a soluble haem-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase.	Defined by 6 residues: LYS:E-56CYS:E-152MET:E-153MET:E-346GLY:E-383GLN:E-384 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.7.99.4 (PDB Primary Data) Search M-CSA Motif + EC 1.7.99.4