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Q50925

- HAO_NITEU

UniProt

Q50925 - HAO_NITEU

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

        10         20         30         40         50
MRIGEWMRGL LLCAGLMMCG VVHADISTVP DETYDALKLD RGKATPKETY
60 70 80 90 100
EALVKRYKDP AHGAGKGTMG DYWEPIAISI YMDPNTFYKP PVSPKEVAER
110 120 130 140 150
KDCVECHSDE TPVWVRAWKR STHANLDKIR NLKSDDPLYY KKGKLEEVEN
160 170 180 190 200
NLRSMGKLGE KETLKEVGCI DCHVDVNKKD KADHTKDIRM PTADTCGTCH
210 220 230 240 250
LREFAERESE RDTMVWPNGQ WPAGRPSHAL DYTANIETTV WAAMPQREVA
260 270 280 290 300
EGCTMCHTNQ NKCDNCHTRH EFSAAESRKP EACATCHSGV DHNNWEAYTM
310 320 330 340 350
SKHGKLAEMN RDKWNWEVRL KDAFSKGGQN APTCAACHME YEGEYTHNIT
360 370 380 390 400
RKTRWANYPF VPGIAENITS DWSEARLDSW VLTCTQCHSE RFARSYLDLM
410 420 430 440 450
DKGTLEGLAK YQEANAIVHK MYEDGTLTGQ KTNRPNPPEP EKPGFGIFTQ
460 470 480 490 500
LFWSKGNNPA SLELKVLEMA ENNLAKMHVG LAHVNPGGWT YTEGWGPMNR
510 520 530 540 550
AYVEIQDEYT KMQELSALQA RVNKLEGKQT SLLDLKGTGE KISLGGLGGG
560 570
MLLAGALALI GWRKRKQTRA
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.
WP_011111571.1. 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.
WP_011111571.1. 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

« Hide 'large scale' publications
  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 29, 2014
This is version 109 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