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Q50925

- HAO_NITEU

UniProt

Q50925 - HAO_NITEU

Protein

Hydroxylamine oxidoreductase

Gene

hao1

more
Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
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    Functioni

    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 activityi

    Hydroxylamine + H2O + 2 ferricytochrome c = nitrite + 2 ferrocytochrome c + 5 H+.
    Hydroxylamine + ferricytochrome c = nitric oxide + ferrocytochrome c + 3 H+.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031Heme 1 (covalent)1 Publication
    Binding sitei106 – 1061Heme 1 (covalent)1 Publication
    Metal bindingi107 – 1071Iron (heme 1 axial ligand)
    Metal bindingi123 – 1231Iron (heme 3 axial ligand)
    Binding sitei169 – 1691Heme 2 (covalent)1 Publication
    Binding sitei172 – 1721Heme 2 (covalent)1 Publication
    Metal bindingi173 – 1731Iron (heme 2 axial ligand)
    Metal bindingi184 – 1841Iron (heme 1 axial ligand)
    Binding sitei196 – 1961Heme 3 (covalent)1 Publication
    Binding sitei199 – 1991Heme 3 (covalent)1 Publication
    Metal bindingi200 – 2001Iron (heme 3 axial ligand)
    Metal bindingi228 – 2281Iron (heme 6 axial ligand)
    Binding sitei253 – 2531Heme 4 (covalent; via 3 links); shared with Y-491 in trimeric partner 1
    Binding sitei256 – 2561Heme 4 (covalent; via 3 links); shared with Y-491 in trimeric partner 1
    Metal bindingi257 – 2571Iron (heme 4 axial ligand)
    Binding sitei263 – 2631Heme 5 (covalent)1 Publication
    Binding sitei266 – 2661Heme 5 (covalent)1 Publication
    Metal bindingi267 – 2671Iron (heme 5 axial ligand)
    Metal bindingi270 – 2701Iron (heme 2 axial ligand)
    Binding sitei283 – 2831Heme 6 (covalent)
    Binding sitei286 – 2861Heme 6 (covalent)1 Publication
    Metal bindingi287 – 2871Iron (heme 6 axial ligand)
    Metal bindingi303 – 3031Iron (heme 8 axial ligand)
    Binding sitei334 – 3341Heme 7 (covalent)1 Publication
    Binding sitei337 – 3371Heme 7 (covalent)1 Publication
    Metal bindingi338 – 3381Iron (heme 7 axial ligand)
    Metal bindingi347 – 3471Iron (heme 5 axial ligand)
    Binding sitei384 – 3841Heme 8 (covalent)1 Publication
    Binding sitei387 – 3871Heme 8 (covalent)1 Publication
    Metal bindingi388 – 3881Iron (heme 8 axial ligand)
    Metal bindingi483 – 4831Iron (heme 7 axial ligand)
    Binding sitei491 – 4911Heme 4 (covalent; via 3 links); shared with C-253 and C-256 in trimeric partner 2

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. oxidoreductase activity Source: CACAO

    GO - Biological processi

    1. anaerobic respiration, using ammonium as electron donor Source: CACAO

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxylamine oxidoreductase (EC:1.7.2.6)
    Short name:
    HAO
    Gene namesi
    Name:hao1
    Ordered Locus Names:NE2044
    AND
    Name:hao2
    Ordered Locus Names:NE0962
    AND
    Name:hao3
    Ordered Locus Names:NE2339
    OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
    Taxonomic identifieri228410 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
    ProteomesiUP000001416: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 570546Hydroxylamine oxidoreductase1 PublicationPRO_0000006604Add
    BLAST

    Post-translational modificationi

    Binds 8 heme groups per subunit.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    STRINGi228410.NE2339.

    Structurei

    Secondary structure

    1
    570
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 366
    Turni41 – 433
    Helixi46 – 5712
    Helixi60 – 623
    Turni68 – 714
    Helixi79 – 824
    Helixi84 – 874
    Helixi100 – 11011
    Helixi112 – 1209
    Helixi122 – 1243
    Helixi126 – 1305
    Helixi137 – 1393
    Helixi140 – 15415
    Helixi169 – 1735
    Turni184 – 1863
    Helixi193 – 1964
    Turni197 – 1993
    Helixi201 – 2088
    Helixi210 – 2134
    Beta strandi226 – 2283
    Helixi231 – 2366
    Helixi239 – 2435
    Helixi247 – 2559
    Turni259 – 2613
    Beta strandi265 – 2673
    Turni269 – 2713
    Helixi274 – 2774
    Helixi280 – 2834
    Turni284 – 2863
    Helixi294 – 3007
    Helixi302 – 3109
    Helixi311 – 3133
    Helixi320 – 3223
    Turni323 – 3275
    Helixi334 – 3385
    Beta strandi339 – 3413
    Turni362 – 3698
    Helixi371 – 38414
    Turni385 – 3873
    Helixi390 – 42334
    Turni428 – 4325
    Helixi448 – 4514
    Helixi461 – 47111
    Helixi473 – 48311
    Helixi486 – 4883
    Turni489 – 4913
    Beta strandi492 – 4943
    Helixi495 – 52531

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ50925.
    SMRiQ50925. Positions 25-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ50925.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85955.
    HOGENOMiHOG000064068.
    KOiK10535.
    OMAiKEDWIAT.
    OrthoDBiEOG6C5RKD.

    Family and domain databases

    InterProiIPR012138. HAO.
    IPR011031. Multihaem_cyt.
    [Graphical view]
    PIRSFiPIRSF000242. HAO. 1 hit.
    PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q50925-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRIGEWMRGL LLCAGLMMCG VVHADISTVP DETYDALKLD RGKATPKETY    50
    EALVKRYKDP AHGAGKGTMG DYWEPIAISI YMDPNTFYKP PVSPKEVAER 100
    KDCVECHSDE TPVWVRAWKR STHANLDKIR NLKSDDPLYY KKGKLEEVEN 150
    NLRSMGKLGE KETLKEVGCI DCHVDVNKKD KADHTKDIRM PTADTCGTCH 200
    LREFAERESE RDTMVWPNGQ WPAGRPSHAL DYTANIETTV WAAMPQREVA 250
    EGCTMCHTNQ NKCDNCHTRH EFSAAESRKP EACATCHSGV DHNNWEAYTM 300
    SKHGKLAEMN RDKWNWEVRL KDAFSKGGQN APTCAACHME YEGEYTHNIT 350
    RKTRWANYPF VPGIAENITS DWSEARLDSW VLTCTQCHSE RFARSYLDLM 400
    DKGTLEGLAK YQEANAIVHK MYEDGTLTGQ KTNRPNPPEP EKPGFGIFTQ 450
    LFWSKGNNPA SLELKVLEMA ENNLAKMHVG LAHVNPGGWT YTEGWGPMNR 500
    AYVEIQDEYT KMQELSALQA RVNKLEGKQT SLLDLKGTGE KISLGGLGGG 550
    MLLAGALALI GWRKRKQTRA 570
    Length:570
    Mass (Da):64,259
    Last modified:May 16, 2003 - v2
    Checksum:iC76AB9019512105E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431A → T in AAC43216. (PubMed:8288544)Curated
    Sequence conflicti470 – 4701A → G in AAC43216. (PubMed:8288544)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04053 Unassigned DNA. Translation: AAC43216.1.
    AL954747 Genomic DNA. Translation: CAD84873.1.
    AL954747 Genomic DNA. Translation: CAD85955.1.
    AL954747 Genomic DNA. Translation: CAD86251.1.
    PIRiA36954.
    RefSeqiNP_841035.1. NC_004757.1.
    NP_842054.1. NC_004757.1.
    NP_842336.1. NC_004757.1.

    Genome annotation databases

    EnsemblBacteriaiCAD84873; CAD84873; NE0962.
    CAD85955; CAD85955; NE2044.
    CAD86251; CAD86251; NE2339.
    GeneIDi1081904.
    1083004.
    1083306.
    KEGGineu:NE0962.
    neu:NE2044.
    neu:NE2339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04053 Unassigned DNA. Translation: AAC43216.1 .
    AL954747 Genomic DNA. Translation: CAD84873.1 .
    AL954747 Genomic DNA. Translation: CAD85955.1 .
    AL954747 Genomic DNA. Translation: CAD86251.1 .
    PIRi A36954.
    RefSeqi NP_841035.1. NC_004757.1.
    NP_842054.1. NC_004757.1.
    NP_842336.1. NC_004757.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FGJ X-ray 2.80 A/B 25-570 [» ]
    4FAS X-ray 2.10 A/B/C 25-570 [» ]
    4N4N X-ray 2.20 A/C/E 25-570 [» ]
    4N4O X-ray 2.47 A/C/E 25-570 [» ]
    ProteinModelPortali Q50925.
    SMRi Q50925. Positions 25-523.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 228410.NE2339.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD84873 ; CAD84873 ; NE0962 .
    CAD85955 ; CAD85955 ; NE2044 .
    CAD86251 ; CAD86251 ; NE2339 .
    GeneIDi 1081904.
    1083004.
    1083306.
    KEGGi neu:NE0962.
    neu:NE2044.
    neu:NE2339.

    Phylogenomic databases

    eggNOGi NOG85955.
    HOGENOMi HOG000064068.
    KOi K10535.
    OMAi KEDWIAT.
    OrthoDBi EOG6C5RKD.

    Enzyme and pathway databases

    BioCyci MetaCyc:HAONITRO-MONOMER.
    NEUR228410:GJNO-2083-MONOMER.
    NEUR228410:GJNO-2384-MONOMER.
    NEUR228410:GJNO-985-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q50925.

    Family and domain databases

    InterProi IPR012138. HAO.
    IPR011031. Multihaem_cyt.
    [Graphical view ]
    PIRSFi PIRSF000242. HAO. 1 hit.
    PROSITEi PS51008. MULTIHEME_CYTC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiHAO_NITEU
    AccessioniPrimary (citable) accession number: Q50925
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3