P0DV45 · NRHAO_KUEST
- ProteinProbable nitrite reductase-hydroxylamine oxidoreductase fusion protein
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids852 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
A nitrite reductase-hydroxylamine oxidoreductase protein that probably functions in the type 1 encapsulin nanocompartment. Probably involved in reductive catalysis. Targeted to the encapsulin nanocompartment by association with the diheme domain of the encapsulin shell protein (AC Q1Q6L7) (Probable). Catalyzes the reduction of nitrite to nitric oxide (NO) (By similarity).
Catalyzes the oxidation of hydroxylamine to nitrite (By similarity).
Catalyzes the oxidation of hydroxylamine to nitrite (By similarity).
Miscellaneous
In (PubMed:28263314) the construct expressed anaerobically in E.coli contains only the nitrite reductase domain (residues 28-327).
Catalytic activity
- 4 Fe(III)-[cytochrome c] + H2O + hydroxylamine = 4 Fe(II)-[cytochrome c] + 5 H+ + nitrite
Cofactor
Protein has several cofactor binding sites:
Note: Binds 8 heme groups per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 102 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 145 | Cu cation 2 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 406 | heme 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 409 | heme 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 410 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 426 | Fe (UniProtKB | ChEBI) of heme 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 463 | heme 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 466 | heme 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 467 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 471 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 483 | heme 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 486 | heme 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 487 | Fe (UniProtKB | ChEBI) of heme 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 505 | Fe (UniProtKB | ChEBI) of heme 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 537 | Fe (UniProtKB | ChEBI) of heme 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 543 | heme 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 546 | heme 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 547 | Fe (UniProtKB | ChEBI) of heme 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 550 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 563 | heme 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 566 | heme 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 567 | Fe (UniProtKB | ChEBI) of heme 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 614 | heme 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 617 | heme 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 618 | Fe (UniProtKB | ChEBI) of heme 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 686 | heme 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 689 | heme 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 690 | Fe (UniProtKB | ChEBI) of heme 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 813 | Fe (UniProtKB | ChEBI) of heme 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | encapsulin nanocompartment | |
Molecular Function | copper ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable nitrite reductase-hydroxylamine oxidoreductase fusion protein
- EC number
- Short namesNIR-HAO
Organism names
- Organism
- Taxonomic lineageBacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Kuenenia
Accessions
- Primary accessionP0DV45
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MLNKSAALVPVVLAFLFLFLCFQCLYA | ||||||
Chain | PRO_0000455329 | 28-852 | Probable nitrite reductase-hydroxylamine oxidoreductase fusion protein | |||
Sequence: DIRCLTGKDGAVHLEMEAKPLTIEPRPGVFFDAWGYCLKGDVPTVPGPVIKVREGTKVKILFRNKLTVPASIHPHGVKYTTANVGVNIAGNPASIVAPGDSRIFEWDTAGTPGTWFYHSYVFERGGEEGLSRGLWGALIVEPVGGDPNPPDKEFVVFMHAFNVNGQEYYAFNNKSGDIELMRGDSSAFPGETWKAKMGDKVRFHLINITEEAHTFHTHGHRWLDKSCDKLIDTIGLNPFDSYVLDFVAGEGVGKGNWAFHCQSQEHMMNGMFGIFMVEEGKRVNAVIASCDEGRKTLSAPGQDRQPPTLEGFSGAYMYPEITEKNMYESFAGLEKGDGIWGDYYSPIPLYTYFNPSRHYVPPESDAYTNLLVKYRPDQCVECHEETTPGIVAEWKMSNHANPKKNPHVSAETQEIEALIGKELNNWRPGTKDGVYCSYCHGSDHEKLFMPTVDNSCGACHPKQAAEFIKGRDHGRPNHPQSWEGNVSTPWYAEYYRRGEGYSMVGCDQCHQNMSSCDDCHSRHRFSAAEARRPEACSICHMGPDHPDWESYSRSKWGVIYETTKERWNWDKNLAEVIPGEDYLAPTCQYCHMYVGNNKWEMNVETKGIWRMGVIPPKEVEFKSGLKDFPYGIKIPPMDKKLEIYSAESQEKRRKWVELCSKCHSSRFAGMWLDSLDQYMFESWRRIDEAQLIIEKLFSENAIEPPPEKRPPFPLSDLIIKVLGAEKLGAEMYRLFKQTNGHLPVIGPILGAYSIFTQNEGNPGGIEREYAEMWFWSHLQGYKGAAHAQPDISWWWGTAQGVGNLTRIRDEAEKLRRLKSGSSSGF |
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-327 | Nitrite reductase domain | ||||
Sequence: DIRCLTGKDGAVHLEMEAKPLTIEPRPGVFFDAWGYCLKGDVPTVPGPVIKVREGTKVKILFRNKLTVPASIHPHGVKYTTANVGVNIAGNPASIVAPGDSRIFEWDTAGTPGTWFYHSYVFERGGEEGLSRGLWGALIVEPVGGDPNPPDKEFVVFMHAFNVNGQEYYAFNNKSGDIELMRGDSSAFPGETWKAKMGDKVRFHLINITEEAHTFHTHGHRWLDKSCDKLIDTIGLNPFDSYVLDFVAGEGVGKGNWAFHCQSQEHMMNGMFGIFMVEEGKRVNAVIASCDEGRKTLSAP | ||||||
Domain | 72-169 | Plastocyanin-like 1 | ||||
Sequence: VPGPVIKVREGTKVKILFRNKLTVPASIHPHGVKYTTANVGVNIAGNPASIVAPGDSRIFEWDTAGTPGTWFYHSYVFERGGEEGLSRGLWGALIVEP | ||||||
Domain | 217-307 | Plastocyanin-like 2 | ||||
Sequence: GETWKAKMGDKVRFHLINITEEAHTFHTHGHRWLDKSCDKLIDTIGLNPFDSYVLDFVAGEGVGKGNWAFHCQSQEHMMNGMFGIFMVEEG | ||||||
Region | 328-827 | Hydroxylamine oxidoreductase domain | ||||
Sequence: GQDRQPPTLEGFSGAYMYPEITEKNMYESFAGLEKGDGIWGDYYSPIPLYTYFNPSRHYVPPESDAYTNLLVKYRPDQCVECHEETTPGIVAEWKMSNHANPKKNPHVSAETQEIEALIGKELNNWRPGTKDGVYCSYCHGSDHEKLFMPTVDNSCGACHPKQAAEFIKGRDHGRPNHPQSWEGNVSTPWYAEYYRRGEGYSMVGCDQCHQNMSSCDDCHSRHRFSAAEARRPEACSICHMGPDHPDWESYSRSKWGVIYETTKERWNWDKNLAEVIPGEDYLAPTCQYCHMYVGNNKWEMNVETKGIWRMGVIPPKEVEFKSGLKDFPYGIKIPPMDKKLEIYSAESQEKRRKWVELCSKCHSSRFAGMWLDSLDQYMFESWRRIDEAQLIIEKLFSENAIEPPPEKRPPFPLSDLIIKVLGAEKLGAEMYRLFKQTNGHLPVIGPILGAYSIFTQNEGNPGGIEREYAEMWFWSHLQGYKGAAHAQPDISWWWGTAQG |
Sequence similarities
In the N-terminal section; belongs to the multicopper oxidase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length852
- Mass (Da)96,352
- Last updated2022-05-25 v1
- ChecksumC8E27B60047708A6