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Reviewed, UniProtKB/Swiss-Prot Q50925 (HAO_NITEU)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hydroxylamine oxidoreductase
      Short name=HAO
    EC=1.7.3.4
Gene names
Name: hao1
Ordered Locus Names: NE2044
AND
Name: hao2
Ordered Locus Names: NE0962
AND
Name: hao3
Ordered Locus Names: NE2339
OrganismNitrosomonas europaea [Complete proteome] [HAMAP]
Taxonomic identifier915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas

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Protein attributes

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

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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 + O2 = nitrite + H2O.

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.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydroxylamine oxidase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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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

1 ........................................................................................ 570
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q50925-1 [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

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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: 8288544] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 19718 / IFO 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: 12700255] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / IFO 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: 9095195] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Strain: ATCC 19718 / IFO 14298.

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Cross-references

Sequence databases

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.
NP_842054.1.
NP_842336.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FGJX-ray2.80A/B25-570[»]
ModBaseSearch...

Genome annotation databases

GeneID1081904.
1083004.
1083306.
GenomeReviewsGene locus NE0962 in contig AL954747_GR.
Gene locus NE2044 in contig AL954747_GR.
Gene locus NE2339 in contig AL954747_GR.
KEGGneu:NE0962.
neu:NE2044.
neu:NE2339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ50925.
OMAQ50925. VETAIWA.

Enzyme and pathway databases

BioCycNEUR228410:NE0962-MON.
NEUR228410:NE2044-MON.
NEUR228410:NE2339-MON.
BRENDA1.7.3.4. 444.

Family and domain databases

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

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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: June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents