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Protein

Hydroxylamine reductase

Gene

hcp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of hydroxylamine to form NH3 and H2O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism.UniRule annotation2 Publications

Catalytic activityi

NH3 + H2O + acceptor = hydroxylamine + reduced acceptor.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by oxygen. Activated by cyanide except in the prolonged presence of excess cyanide, where the enzyme is inactivated.1 Publication

Kineticsi

  1. KM=2.5 mM for hydroxylamine (at pH 9)1 Publication
  1. Vmax=92 µmol/min/mg enzyme (at pH 7.5)1 Publication
  2. Vmax=458 µmol/min/mg enzyme (at pH 9)1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi3 – 31Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi6 – 61Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi18 – 181Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi25 – 251Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi75 – 751Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi249 – 2491Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogenUniRule annotation
Metal bindingi273 – 2731Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi317 – 3171Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi405 – 4051Iron-oxo-sulfur (4Fe-2O-2S); via persulfide groupUniRule annotation
Metal bindingi433 – 4331Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi458 – 4581Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi492 – 4921Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi494 – 4941Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • hydroxylamine reductase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: EcoliWiki
  • peroxidase activity Source: EcoliWiki

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • nitrogen compound metabolic process Source: EcoCyc
  • oxidation-reduction process Source: EcoliWiki
  • response to hydrogen peroxide Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6457-MONOMER.
ECOL316407:JW0857-MONOMER.
MetaCyc:G6457-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxylamine reductase1 Publication (EC:1.7.99.11 Publication)
Alternative name(s):
Hybrid-cluster proteinUniRule annotation
Short name:
HCPUniRule annotation
Prismane protein1 Publication
Gene namesi
Name:hcpUniRule annotation
Synonyms:ybjW
Ordered Locus Names:b0873, JW0857
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13692. hcp.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550Hydroxylamine reductasePRO_0000151674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei405 – 4051Cysteine persulfideUniRule annotation

Proteomic databases

PaxDbiP75825.
PRIDEiP75825.

Expressioni

Inductioni

By Fnr, NarL and NarP under anaerobic conditions in the presence of either nitrate or nitrite.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
poxBP070031EBI-561591,EBI-909338

Protein-protein interaction databases

BioGridi4262100. 10 interactions.
DIPiDIP-9870N.
IntActiP75825. 5 interactions.
STRINGi511145.b0873.

Structurei

3D structure databases

ProteinModelPortaliP75825.
SMRiP75825. Positions 1-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HCP family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000007176.
InParanoidiP75825.
KOiK05601.
OMAiCAYAQGM.
OrthoDBiEOG69WFJT.
PhylomeDBiP75825.

Family and domain databases

Gene3Di1.20.1270.20. 2 hits.
3.40.50.2030. 2 hits.
HAMAPiMF_00069. Hydroxylam_reduct.
InterProiIPR004137. HCP/CODH.
IPR010048. Hydroxylam_reduct.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
IPR016100. Prismane_a-bundle.
[Graphical view]
PfamiPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFiPIRSF000076. HCP. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01703. hybrid_clust. 1 hit.

Sequencei

Sequence statusi: Complete.

P75825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFCVQCEQTI RTPAGNGCSY AQGMCGKTAE TSDLQDLLIA ALQGLSAWAV
60 70 80 90 100
KAREYGIINH DVDSFAPRAF FSTLTNVNFD SPRIVGYARE AIALREALKA
110 120 130 140 150
QCLAVDANAR VDNPMADLQL VSDDLGELQR QAAEFTPNKD KAAIGENILG
160 170 180 190 200
LRLLCLYGLK GAAAYMEHAH VLGQYDNDIY AQYHKIMAWL GTWPADMNAL
210 220 230 240 250
LECSMEIGQM NFKVMSILDA GETGKYGHPT PTQVNVKATA GKCILISGHD
260 270 280 290 300
LKDLYNLLEQ TEGTGVNVYT HGEMLPAHGY PELRKFKHLV GNYGSGWQNQ
310 320 330 340 350
QVEFARFPGP IVMTSNCIID PTVGAYDDRI WTRSIVGWPG VRHLDGDDFS
360 370 380 390 400
AVITQAQQMA GFPYSEIPHL ITVGFGRQTL LGAADTLIDL VSREKLRHIF
410 420 430 440 450
LLGGCDGARG ERHYFTDFAT SVPDDCLILT LACGKYRFNK LEFGDIEGLP
460 470 480 490 500
RLVDAGQCND AYSAIILAVT LAEKLGCGVN DLPLSLVLSW FEQKAIVILL
510 520 530 540 550
TLLSLGVKNI VTGPTAPGFL TPDLLAVLNE KFGLRSITTV EEDMKQLLSA
Length:550
Mass (Da):60,064
Last modified:May 30, 2000 - v2
Checksum:iCA4958B3143B1F48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341E → V in AAC73960 (PubMed:8905232).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73960.2.
AP009048 Genomic DNA. Translation: BAA35587.2.
PIRiA64826.
RefSeqiNP_415394.4. NC_000913.3.
WP_000458809.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73960; AAC73960; b0873.
BAA35587; BAA35587; BAA35587.
GeneIDi946592.
KEGGiecj:JW0857.
eco:b0873.
PATRICi32116953. VBIEscCol129921_0902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73960.2.
AP009048 Genomic DNA. Translation: BAA35587.2.
PIRiA64826.
RefSeqiNP_415394.4. NC_000913.3.
WP_000458809.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP75825.
SMRiP75825. Positions 1-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262100. 10 interactions.
DIPiDIP-9870N.
IntActiP75825. 5 interactions.
STRINGi511145.b0873.

Proteomic databases

PaxDbiP75825.
PRIDEiP75825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73960; AAC73960; b0873.
BAA35587; BAA35587; BAA35587.
GeneIDi946592.
KEGGiecj:JW0857.
eco:b0873.
PATRICi32116953. VBIEscCol129921_0902.

Organism-specific databases

EchoBASEiEB3456.
EcoGeneiEG13692. hcp.

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000007176.
InParanoidiP75825.
KOiK05601.
OMAiCAYAQGM.
OrthoDBiEOG69WFJT.
PhylomeDBiP75825.

Enzyme and pathway databases

BioCyciEcoCyc:G6457-MONOMER.
ECOL316407:JW0857-MONOMER.
MetaCyc:G6457-MONOMER.

Miscellaneous databases

PROiP75825.

Family and domain databases

Gene3Di1.20.1270.20. 2 hits.
3.40.50.2030. 2 hits.
HAMAPiMF_00069. Hydroxylam_reduct.
InterProiIPR004137. HCP/CODH.
IPR010048. Hydroxylam_reduct.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
IPR016100. Prismane_a-bundle.
[Graphical view]
PfamiPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFiPIRSF000076. HCP. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01703. hybrid_clust. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 134.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Biochemical and spectroscopic characterization of overexpressed fuscoredoxin from Escherichia coli."
    Pereira A.S., Tavares P., Krebs C., Huynh B.H., Rusnak F., Moura I., Moura J.J.
    Biochem. Biophys. Res. Commun. 260:209-215(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  5. "The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and 2Fe-2S."
    van den Berg W.A.M., Hagen W.R., van Dongen W.M.A.M.
    Eur. J. Biochem. 267:666-676(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  6. "Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli."
    Wolfe M.T., Heo J., Garavelli J.S., Ludden P.W.
    J. Bacteriol. 184:5898-5902(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
  7. "Transcriptional regulation of a hybrid cluster (prismane) protein."
    Filenko N.A., Browning D.F., Cole J.A.
    Biochem. Soc. Trans. 33:195-197(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiHCP_ECOLI
AccessioniPrimary (citable) accession number: P75825
Secondary accession number(s): Q9R7R0, Q9R7R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: February 17, 2016
This is version 133 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.