Structure of PDB 1fgj Chain B

Receptor sequence
>1fgjB (length=499) Species: 915 (Nitrosomonas europaea) [Search protein sequence]
DISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWE
PIAISIYMDPNTFYKPPVSPKEVAERKDCVECHSDETPVWVRAWKRSTHA
NLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHV
DVNKKDKADHTKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAG
RPSHALDYTANIETTVWATMPQREVAEGCTMCHTNQNKCDNCHTRHEFSA
AESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRLKDAF
SKGGQNAPTCAACHMEYEGEYTHNITRKTRWANYPFVPGIAENITSDWSE
ARLDSWVLTCTQCHSERFARSYLDLMDKGTLEGLAKYQEANAIVHKMYED
GTLTGQKTNRPNPPEPEKPGFGIFTQLFWSKGNNPASLELKVLEMGENNL
AKMHVGLAHVNPGGWTYTEGWGPMNRAYVEIQDEYTKMQELSALQARVN
3D structure
PDB1fgj The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea.
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H233 D267 H268 Y334 Y467
Catalytic site (residue number reindexed from 1) H233 D267 H268 Y334 Y467
Enzyme Commision number 1.7.2.6: hydroxylamine dehydrogenase.
1.7.2.9: hydroxylamine oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0033740 hydroxylamine oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0047991 hydroxylamine oxidase activity
Biological Process
GO:0019331 anaerobic respiration, using ammonium as electron donor
GO:0070207 protein homotrimerization
Cellular Component
GO:0044222 anammoxosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1fgj, PDBe:1fgj, PDBj:1fgj
PDBsum1fgj
PubMed9095195
UniProtQ50925|HAO_NITEU Hydroxylamine oxidoreductase (Gene Name=hao1)

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