1NIA

THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED

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	d1niaa2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Achromobacter cycloclastes ) [TaxId: 223 ],	SCOPe (2.08)
A	d1niaa1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Achromobacter cycloclastes ) [TaxId: 223 ],	SCOPe (2.08)
B	d1niab2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Achromobacter cycloclastes ) [TaxId: 223 ],	SCOPe (2.08)
B	d1niab1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Achromobacter cycloclastes ) [TaxId: 223 ],	SCOPe (2.08)
C	d1niac2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, C-terminal domain	(Achromobacter cycloclastes ) [TaxId: 223 ],	SCOPe (2.08)
C	d1niac1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Nitrite reductase, NIR, N-terminal domain	(Achromobacter cycloclastes ) [TaxId: 223 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cupredoxins	8038727	3000886	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cupredoxins	8038726	3000886	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cupredoxins	8038726	3000886	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cupredoxins	8038727	3000886	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cupredoxins	8038727	3000886	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cupredoxins	8038726	3000886	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	Cu-oxidase_2_2	e1niaA2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
A	Cu-oxidase_3_1	e1niaA1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
B	Cu-oxidase_2_2	e1niaB2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
B	Cu-oxidase_3_1	e1niaB1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)
C	Cu-oxidase_2_2	e1niaC2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2_2	ECOD (1.6)
C	Cu-oxidase_3_1	e1niaC1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
B	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)
C	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00394	Multicopper oxidase (Cu-oxidase)	Multicopper oxidase	Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.	Domain
A, B, C	PF07732	Multicopper oxidase (Cu-oxidase_3)	Multicopper oxidase	This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	NITRITE REDUCTASE	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor oxidoreductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors nitrite reductase (NO-forming) activity nitrite reductase activity catalytic activity	nitrogen cycle metabolic process denitrification pathway metabolic process cellular process nitrate assimilation oxoacid metabolic process small molecule metabolic process organic acid metabolic process nitrate metabolic process reactive nitrogen species metabolic process	cellular anatomical structure periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, B, C	IPR008972	Cupredoxin	Homologous Superfamily
A, B, C	IPR001117	Multicopper oxidase, second cupredoxin domain	Domain
A, B, C	IPR001287	Nitrite reductase, copper-type	Family
A, B, C	IPR011707	Multicopper oxidase-like, N-terminal	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A, B	nitrite reductase (copper type) M-CSA #4	This family of enzymes is found in both denitrifying bacteria and fungi which reside in soil and aquatic ecosystems. Denitrification, the reduction of dissolved nitrate and nitrite to gaseous NO, N₂0 and N₂ is an important process in the recycling of nitrogen in the biosphere, and is a key step in the nitrogen cycle resulting in the loss of terrestrial nitrogen to the atmosphere. It is chiefly carried out by denitrifying bacteria, which contain nitrate and nitrite reductases. The copper-containing family of enzymes is found in both denitrifying bacteria and fungi which reside in soil and aquatic ecosystems and uses copper ions as cofactors rather than the more common haem cd1 The enzymes in question catalyse the reduction of nitrite (NO₂^-) to NO + H₂O. They contain two copper centres, a Type I centre which receives electrons from pseudoazurin (a copper containing protein), and a type II centre which is the site of nitrite reduction.	Defined by 11 residues: HIS:A-95ASP:A-98HIS:A-100HIS:A-135CYS:A-136HIS:A-145MET:A-150HIS:B-255GLU:B-279THR:B-280HIS:B-306 \| Explore in 3D: M-CSA Motif Definition Up to 10 residues are supported for Structure Motif searching, this motif has 11 residues. EC: 1.7.99.3 (PDB Primary Data) EC: 1.7.2.1 (UniProt)

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.