Q1Q0T2 · HZSA_KUEST
- ProteinHydrazine synthase subunit alpha
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids809 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine (PubMed:21964329).
The alpha subunit catalyzes the second half-reaction, i.e. the condensation of hydroxylamine formed in the active site of the gamma subunit with ammonia, yielding hydrazine (PubMed:26479033).
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, PubMed:26479033).
The alpha subunit catalyzes the second half-reaction, i.e. the condensation of hydroxylamine formed in the active site of the gamma subunit with ammonia, yielding hydrazine (PubMed:26479033).
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, PubMed:26479033).
Catalytic activity
- 3 Fe(III)-[cytochrome c] + H2O + hydrazine = 3 Fe(II)-[cytochrome c] + 2 H+ + NH4+ + nitric oxide
Cofactor
Note: Binds two heme c groups per subunit.
Pathway
Nitrogen metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 303 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 583 | heme 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 586 | heme 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 587 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 591 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Y | ||||||
Binding site | 685 | heme 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 688 | heme 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 689 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 772 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | anammoxosome | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHydrazine synthase subunit alpha
- EC number
- Short namesHZS-alpha
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Kuenenia
Accessions
- Primary accessionQ1Q0T2
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MGKRKLGVIASAFVAGALVCGSTLVNA | ||||||
Chain | PRO_5004195495 | 28-809 | Hydrazine synthase subunit alpha | |||
Sequence: EPVMTGGPVQGKALWTDYSGMSKEVQGPVSQILFTQSPRTAKGDPYQNYPHYIPEGSRIVLFDLNTKELKVLTNDFATAFDPCTYWDGKKFAFAGVHKKGGGCQIWEMNIDGSGLRQMTDLKGTCRSPIYYAAGSIEEGEGRIIWRDRYFEGDWKEHGMVEKTGMIIFSGSPEGVMDEFHNPYAYNLYRLDTQGGKIIQRITGHVLSGIEFPHLNTTIDQITYNLSSNFDPWLTPDGNILFSSVQANGSRAGGEGRVMICVDNWDGAYPRPIYGNCDGEIGGTSGRSQAKITFGDRKIVYVESPYMNWGVGQLAAVSWDAPFNKTYEKLTGKDGGLYRSPYPLPDDRMLVSYAERGDFGIYWFNFSKCAAGDKVYDDPNWNDHQPAPVYVKYKPRWINTFTAGKNFGVTVVTYQPFDQVKVEGYPHSWGTWICFDTTLSDQPVGPYPHQKAKNVSHGDIKAVRIIQGYQCVEPDSTRFRVGAGAHLLGGERSSSNSGTAFQQRGIIGYQYVESDGSTVTSQLSDVPYYMQILDDKGMSVQTALTWAYLRPYHGRICSGCHYGSYRGRAFKNIHAKALYNWWYDDRSHYDSPFAFRYLKFDNDGNYKGVKHGEDVVVPSDIYYGGPSGTTSQPVEGLTLDKQRTVDFRRDIQPILDAKCAMCHDSNNPPNLGGGLELVSVDGIAAYSRAYNSLLEPQRGKDPNIGGKYVNPSAAINSLLVWRLYEAELSANAPREKIFPIEGRLLHNKFLTQDERYAIVEWIDLGAQWDNIPGPDFYPGYLVK |
Expression
Induction
Is among the most highly expressed proteins in the proteome.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 633-792 | Cytochrome c | ||||
Sequence: KGVKHGEDVVVPSDIYYGGPSGTTSQPVEGLTLDKQRTVDFRRDIQPILDAKCAMCHDSNNPPNLGGGLELVSVDGIAAYSRAYNSLLEPQRGKDPNIGGKYVNPSAAINSLLVWRLYEAELSANAPREKIFPIEGRLLHNKFLTQDERYAIVEWIDLGA |
Domain
The alpha subunit consists of three domains: an N-terminal domain which includes a six-bladed beta-propeller, a middle domain binding a pentacoordinated c-type heme and a C-terminal domain which harbors a bis-histidine-coordinated c-type heme.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length809
- Mass (Da)90,244
- Last updated2006-05-16 v1
- Checksum4D60D075EB87A7CF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CT573071 EMBL· GenBank· DDBJ | CAJ73613.1 EMBL· GenBank· DDBJ | Genomic DNA |