Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q50925 (HAO_NITEU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxylamine oxidoreductase

Short name=HAO
EC=1.7.2.6
Gene names
Name:hao1
Ordered Locus Names:NE2044
AND
Name:hao2
Ordered Locus Names:NE0962
AND
Name:hao3
Ordered Locus Names:NE2339
OrganismNitrosomonas europaea (strain ATCC 19718 / NBRC 14298) [Complete proteome] [HAMAP]
Taxonomic identifier228410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of hydroxylamine to nitrite. The electrons released in the reaction are partitioned to ammonium monooxygenase and to the respiratory chain. The immediate acceptor of electrons from HAO is cytochrome c-554.

Catalytic activity

Hydroxylamine + H2O + 2 ferricytochrome c = nitrite + 2 ferrocytochrome c + 5 H+.

Hydroxylamine + ferricytochrome c = nitric oxide + ferrocytochrome c + 3 H+.

Cofactor

Binds 8 heme groups per subunit. One heme group a p-460 type, the remaining 7 are c-type.

Subunit structure

Homotrimer.

Subcellular location

Periplasm.

Post-translational modification

Binds 8 heme groups per subunit.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processanaerobic respiration, using ammonium as electron donor

Inferred from direct assay PubMed 9453157. Source: CACAO

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity

Inferred from direct assay PubMed 227845. Source: CACAO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 570546Hydroxylamine oxidoreductase Ref.1
PRO_0000006604

Sites

Metal binding1071Iron (heme 1 axial ligand)
Metal binding1231Iron (heme 3 axial ligand)
Metal binding1731Iron (heme 2 axial ligand)
Metal binding1841Iron (heme 1 axial ligand)
Metal binding2001Iron (heme 3 axial ligand)
Metal binding2281Iron (heme 6 axial ligand)
Metal binding2571Iron (heme 4 axial ligand)
Metal binding2671Iron (heme 5 axial ligand)
Metal binding2701Iron (heme 2 axial ligand)
Metal binding2871Iron (heme 6 axial ligand)
Metal binding3031Iron (heme 8 axial ligand)
Metal binding3381Iron (heme 7 axial ligand)
Metal binding3471Iron (heme 5 axial ligand)
Metal binding3881Iron (heme 8 axial ligand)
Metal binding4831Iron (heme 7 axial ligand)
Binding site1031Heme 1 (covalent) Ref.3
Binding site1061Heme 1 (covalent) Ref.3
Binding site1691Heme 2 (covalent) Ref.3
Binding site1721Heme 2 (covalent) Ref.3
Binding site1961Heme 3 (covalent) Ref.3
Binding site1991Heme 3 (covalent) Ref.3
Binding site2531Heme 4 (covalent; via 3 links); shared with Y-491 in trimeric partner 1
Binding site2561Heme 4 (covalent; via 3 links); shared with Y-491 in trimeric partner 1
Binding site2631Heme 5 (covalent) Ref.3
Binding site2661Heme 5 (covalent) Ref.3
Binding site2831Heme 6 (covalent)
Binding site2861Heme 6 (covalent) Ref.3
Binding site3341Heme 7 (covalent) Ref.3
Binding site3371Heme 7 (covalent) Ref.3
Binding site3841Heme 8 (covalent) Ref.3
Binding site3871Heme 8 (covalent) Ref.3
Binding site4911Heme 4 (covalent; via 3 links); shared with C-253 and C-256 in trimeric partner 2

Experimental info

Sequence conflict2431A → T in AAC43216. Ref.1
Sequence conflict4701A → G in AAC43216. Ref.1

Secondary structure

....................................................................................... 570
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q50925 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: C76AB9019512105E

FASTA57064,259
        10         20         30         40         50         60 
MRIGEWMRGL LLCAGLMMCG VVHADISTVP DETYDALKLD RGKATPKETY EALVKRYKDP 

        70         80         90        100        110        120 
AHGAGKGTMG DYWEPIAISI YMDPNTFYKP PVSPKEVAER KDCVECHSDE TPVWVRAWKR 

       130        140        150        160        170        180 
STHANLDKIR NLKSDDPLYY KKGKLEEVEN NLRSMGKLGE KETLKEVGCI DCHVDVNKKD 

       190        200        210        220        230        240 
KADHTKDIRM PTADTCGTCH LREFAERESE RDTMVWPNGQ WPAGRPSHAL DYTANIETTV 

       250        260        270        280        290        300 
WAAMPQREVA EGCTMCHTNQ NKCDNCHTRH EFSAAESRKP EACATCHSGV DHNNWEAYTM 

       310        320        330        340        350        360 
SKHGKLAEMN RDKWNWEVRL KDAFSKGGQN APTCAACHME YEGEYTHNIT RKTRWANYPF 

       370        380        390        400        410        420 
VPGIAENITS DWSEARLDSW VLTCTQCHSE RFARSYLDLM DKGTLEGLAK YQEANAIVHK 

       430        440        450        460        470        480 
MYEDGTLTGQ KTNRPNPPEP EKPGFGIFTQ LFWSKGNNPA SLELKVLEMA ENNLAKMHVG 

       490        500        510        520        530        540 
LAHVNPGGWT YTEGWGPMNR AYVEIQDEYT KMQELSALQA RVNKLEGKQT SLLDLKGTGE 

       550        560        570 
KISLGGLGGG MLLAGALALI GWRKRKQTRA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea."
Sayavedra-Soto L.A., Hommes N.G., Arp D.J.
J. Bacteriol. 176:504-510(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 19718 / NBRC 14298.
[2]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / NBRC 14298.
[3]"The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea."
Igarashi N., Moriyama H., Fujiwara T., Fukumori Y., Tanaka N.
Nat. Struct. Biol. 4:276-284(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Strain: ATCC 19718 / NBRC 14298.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04053 Unassigned DNA. Translation: AAC43216.1.
AL954747 Genomic DNA. Translation: CAD84873.1.
AL954747 Genomic DNA. Translation: CAD85955.1.
AL954747 Genomic DNA. Translation: CAD86251.1.
PIRA36954.
RefSeqNP_841035.1. NC_004757.1.
NP_842054.1. NC_004757.1.
NP_842336.1. NC_004757.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FGJX-ray2.80A/B25-570[»]
4FASX-ray2.10A/B/C25-570[»]
4N4NX-ray2.20A/C/E25-570[»]
4N4OX-ray2.47A/C/E25-570[»]
ProteinModelPortalQ50925.
SMRQ50925. Positions 25-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228410.NE2339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD84873; CAD84873; NE0962.
CAD85955; CAD85955; NE2044.
CAD86251; CAD86251; NE2339.
GeneID1081904.
1083004.
1083306.
KEGGneu:NE0962.
neu:NE2044.
neu:NE2339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG85955.
HOGENOMHOG000064068.
KOK10535.
OMACHTRHTF.
OrthoDBEOG6C5RKD.
ProtClustDBCLSK585568.

Enzyme and pathway databases

BioCycMetaCyc:HAONITRO-MONOMER.
NEUR228410:GJNO-2083-MONOMER.
NEUR228410:GJNO-2384-MONOMER.
NEUR228410:GJNO-985-MONOMER.

Family and domain databases

InterProIPR012138. HAO.
IPR011031. Multihaem_cyt.
[Graphical view]
PIRSFPIRSF000242. HAO. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ50925.

Entry information

Entry nameHAO_NITEU
AccessionPrimary (citable) accession number: Q50925
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 16, 2003
Last modified: March 19, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references