Q1PW30 · HDH_KUEST
- ProteinHydrazine dehydrogenase
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids582 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329).
The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799).
Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329).
Cannot oxidize hydroxylamine to NO (PubMed:21964329).
The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799).
Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329).
Cannot oxidize hydroxylamine to NO (PubMed:21964329).
Catalytic activity
- 4 Fe(III)-[cytochrome c] + hydrazine = 4 Fe(II)-[cytochrome c] + 4 H+ + N2
Cofactor
Note: Binds 8 heme c groups per subunit (PubMed:31001586).
One of them, heme-4, is an atypical heme c (unusual heme c binding motif CXXXXCH) and is called P460 (PubMed:31001586).
Catalysis takes place at heme-4/P460 (PubMed:31001586).
The other c-type hemes mediate electron transfer to the external electron acceptor, which is a cytochrome c-type protein (PubMed:31001586).
One of them, heme-4, is an atypical heme c (unusual heme c binding motif CXXXXCH) and is called P460 (PubMed:31001586).
Catalysis takes place at heme-4/P460 (PubMed:31001586).
The other c-type hemes mediate electron transfer to the external electron acceptor, which is a cytochrome c-type protein (PubMed:31001586).
Activity regulation
Is strongly and competitively inhibited by NO and hydroxylamine.
Pathway
Nitrogen metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 121 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 124 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 125 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 141 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 151 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 154 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 155 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 159 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 170 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 175 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 176 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 191 | Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 216 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 219 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 220 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 227 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 230 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 231 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 234 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 247 | heme c 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 250 | heme c 6 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 251 | Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 267 | Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 297 | heme c 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 300 | heme c 7 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 301 | Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 306 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 342 | heme c 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 345 | heme c 8 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 346 | Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 454 | Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 462 | heme c 4 (UniProtKB | ChEBI); covalent; ligand shared between tetrameric partners | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | anammoxosome | |
Molecular Function | heme binding | |
Molecular Function | hydroxylamine oxidoreductase activity | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Biological Process | protein homotrimerization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHydrazine dehydrogenase
- EC number
- Short namesHDH
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Kuenenia
Accessions
- Primary accessionQ1PW30
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MRKFLKVTLASALIGCGVIGTVSSLMVKEAKA | ||||||
Chain | PRO_0000441263 | 33-582 | Hydrazine dehydrogenase | |||
Sequence: VEIITHWVPHEVYGMPGEPDNSGKVFFSGLKAKYMGYPKDAQRSPYPGKYSKFWKTLPAYRYYIPDYMYNRDEVRPSNPIKGTFKLEQCVACHSVMTPGIVRDYNKSAHSKAEPAPTGCDTCHGNNHQKLTMPSSKACGTAECHETQYNEQGQGGIGSHASCSSFAQVECAWSIERPPGDTAGCTFCHTSPEERCSTCHQRHQFDPAVARRSEQCKTCHWGKDHRDWEAYDIGLHGTVYQVNKWDTEQFDFSKKLSDADYVGPTCQYCHMRGGHHNVQRASIVYTSMGMSMADRGAPLWKEKRDRWVSICDDCHSPRFARENLQAMDESVKDASLKYRETFKVAEDLLIDGVLDPMPKDLCPDWSGQHIWSLKIGAYHDGEAYGGTTGESGEFRMSNCTDVERLCFESVGYFQTYIYKGMAHGSWNDATYSDGSFGMDRWLVNVKQNASRARRLAALEKKVGISWQPEQFWKTGEWLDQLTGPYIVKNHPGKTIFDLCPDPGWLDTHHAPAEEVEYIERKLKELGITAGSHSAHHHESGHDPAARSMKEH |
Expression
Induction
Is highly expressed (at protein level).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length582
- Mass (Da)65,577
- Last updated2017-08-30 v2
- Checksum3006EE78AC726B96
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CT573073 EMBL· GenBank· DDBJ | CAJ71439.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |