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UniProtKB/Swiss-Prot entry Q50925

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HAO_NITEU
Primary accession number Q50925
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on May 16, 2003 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 70)
Name and origin of the protein
Protein name Hydroxylamine oxidoreductase [Precursor]
Synonyms HAO
EC 1.7.3.4
Gene names
Name: hao1
OrderedLocusNames: NE2044
and
Name: hao2
OrderedLocusNames: NE0962
and
Name: hao3
OrderedLocusNames: NE2339
From
Nitrosomonas europaea [TaxID: 915] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 19718 / IFO 14298;
PubMed=8288544 [NCBI, ExPASy, EBI, Israel, Japan]
Sayavedra-Soto L.A., Hommes N.G., Arp D.J.;
"Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea.";
J. Bacteriol. 176:504-510(1994).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 19718 / IFO 14298;
DOI=10.1128/JB.185.9.2759-2773.2003; PubMed=12700255 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea.";
J. Bacteriol. 185:2759-2773(2003).
[3]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
STRAIN=ATCC 19718 / IFO 14298;
DOI=10.1038/nsb0497-276; PubMed=9095195 [NCBI, ExPASy, EBI, Israel, Japan]
Igarashi N., Moriyama H., Fujiwara T., Fukumori Y., Tanaka N.;
"The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea.";
Nat. Struct. Biol. 4:276-284(1997).
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: Homotrimer.
  • SUBCELLULAR LOCATION: Periplasm.
  • PTM: Binds 8 heme groups per subunit.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U04053; AAC43216.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954747; CAD84873.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954747; CAD85955.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954747; CAD86251.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A36954; A36954.
RefSeq NP_841035.1; -.
NP_842054.1; -.
NP_842336.1; -.
3D structure databases
PDB
1FGJ; X-ray; 2.80 A; A/B=25-570.[ExPASy / RCSB / EBI]
PDBsum 1FGJ; -.
ModBase Q50925.
Enzyme and pathway databases
BioCyc NEUR228410:NE0962-MON; -.
NEUR228410:NE2044-MON; -.
NEUR228410:NE2339-MON; -.
Family and domain databases
InterPro IPR012138; HAO.
IPR001611; LRR.
IPR011031; Multihaem_cyt.
Graphical view of domain structure.
PIRSF PIRSF000242; HAO; 1.
PRINTS PR00019; LEURICHRPT.
PROSITE PS51008; MULTIHEME_CYTC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q50925.
Genome annotation databases
GeneID 1081904; -.
1083004; -.
1083306; -.
GenomeReviews AL954747_GR; NE0962.
AL954747_GR; NE2044.
AL954747_GR; NE2339.
KEGG neu:NE0962; -.
neu:NE2044; -.
neu:NE2339; -.
Phylogenomic databases
HOGENOM Q50925; -.
Other
LinkHub Q50925; -.
Genome annotation databases
CMR Q50925; NE2044.
Other
ProtoNet Q50925.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    24  24      
CHAIN   25   570  546     Hydroxylamine oxidoreductase. PRO_0000006604
METAL   107   107        Iron (heme 1 axial ligand). 
METAL   123   123        Iron (heme 3 axial ligand). 
METAL   173   173        Iron (heme 2 axial ligand). 
METAL   184   184        Iron (heme 1 axial ligand). 
METAL   200   200        Iron (heme 3 axial ligand). 
METAL   228   228        Iron (heme 6 axial ligand). 
METAL   257   257        Iron (heme 4 axial ligand). 
METAL   267   267        Iron (heme 5 axial ligand). 
METAL   270   270        Iron (heme 2 axial ligand). 
METAL   287   287        Iron (heme 6 axial ligand). 
METAL   303   303        Iron (heme 8 axial ligand). 
METAL   338   338        Iron (heme 7 axial ligand). 
METAL   347   347        Iron (heme 5 axial ligand). 
METAL   388   388        Iron (heme 8 axial ligand). 
METAL   483   483        Iron (heme 7 axial ligand). 
BINDING   103   103        Heme 1 (covalent). 
BINDING   106   106        Heme 1 (covalent). 
BINDING   169   169        Heme 2 (covalent). 
BINDING   172   172        Heme 2 (covalent). 
BINDING   196   196        Heme 3 (covalent). 
BINDING   199   199        Heme 3 (covalent). 
BINDING   253   253        Heme 4 (covalent; via 3 links); shared with Y-491 in trimeric partner 1. 
BINDING   256   256        Heme 4 (covalent; via 3 links); shared with Y-491 in trimeric partner 1. 
BINDING   263   263        Heme 5 (covalent). 
BINDING   266   266        Heme 5 (covalent). 
BINDING   283   283        Heme 6 (covalent). 
BINDING   286   286        Heme 6 (covalent). 
BINDING   334   334        Heme 7 (covalent). 
BINDING   337   337        Heme 7 (covalent). 
BINDING   384   384        Heme 8 (covalent). 
BINDING   387   387        Heme 8 (covalent). 
BINDING   491   491        Heme 4 (covalent; via 3 links); shared with C-253 and C-256 in trimeric partner 2. 
CONFLICT   243   243        A -> T (in Ref. 1; AAC43216). 
CONFLICT   470   470        A -> G (in Ref. 1; AAC43216). 
HELIX   31    37  7      
TURN   41    43  3      
HELIX   46    58  13      
HELIX   60    62  3      
HELIX   70    72  3      
HELIX   79    82  4      
HELIX   84    87  4      
HELIX   100   110  11      
HELIX   112   119  8      
TURN   122   124  3      
HELIX   126   130  5      
HELIX   137   139  3      
HELIX   140   154  15      
HELIX   169   173  5      
HELIX   184   187  4      
HELIX   193   197  5      
HELIX   201   208  8      
HELIX   210   213  4      
STRAND   226   228  3      
HELIX   231   236  6      
HELIX   239   243  5      
HELIX   247   254  8      
TURN   259   261  3      
TURN   264   266  3      
TURN   269   271  3      
HELIX   274   278  5      
HELIX   280   282  3      
TURN   283   286  4      
HELIX   294   300  7      
HELIX   302   310  9      
TURN   311   313  3      
HELIX   320   323  4      
TURN   324   326  3      
HELIX   334   338  5      
STRAND   339   343  5      
TURN   362   364  3      
HELIX   365   369  5      
HELIX   371   384  14      
TURN   385   387  3      
HELIX   390   423  34      
STRAND   430   433  4      
HELIX   448   451  4      
HELIX   461   471  11      
HELIX   473   482  10      
HELIX   486   488  3      
STRAND   490   493  4      
HELIX   495   522  28      
Sequence information
Length: 570 AA [This is the length of the unprocessed precursor] Molecular weight: 64259 Da [This is the MW of the unprocessed precursor] CRC64: C76AB9019512105E [This is a checksum on the sequence] 
        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
Q50925 in FASTA format

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