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PMID:19558586

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Citation

Karlsson, R, Karlsson, A, Bäckman, O, Johansson, BR and Hulth, S (2009) Identification of key proteins involved in the anammox reaction. FEMS Microbiol. Lett. 297:87-94

Abstract

Bacteria performing anaerobic ammonium oxidation (anammox) are key players in the global nitrogen cycle due to their inherent ability to convert biologically available nitrogen to N(2). Anammox is increasingly being exploited during wastewater treatment worldwide, and about 50% of the total N(2) production in marine environments is estimated to proceed by the anammox pathway. To fully understand the microbial functionality and mechanisms that control environmental feedbacks of the anammox reaction, key proteins involved in the reaction must be identified. In this study we have utilized an analytical protocol that facilitates detection of proteins associated with the anammoxosome, an intracellular membrane compartment within the anammox bacterium. The protocol enabled us to identify several key proteins of the anammox reaction including a hydrazine hydrolase producing hydrazine, a hydrazine-oxidizing enzyme converting hydrazine to N(2) and a membrane-bound ATP synthase generating ATP from the gradients of protons formed in the anammox reaction. We also performed immunogold labelling electron microscopy to determine the subcellular location of the hydrazine hydrolase. The results from our study support the hypothesis that proteins associated with the anammoxosome host the complete suite of reactions during anammox.

Links

PubMed Online version:10.1111/j.1574-6968.2009.01677.x

Keywords

Anaerobiosis; Bacteria/enzymology; Bacteria/genetics; Bacteria/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Hydrazines/metabolism; Nitrogen/metabolism; Oxidation-Reduction; Quaternary Ammonium Compounds/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

9BACT:Q1Q0T3

GO:0044222: anammoxosome

ECO:0000314:

C

Results: "The anammoxosomes of intact bacteria were invariably labelled with the anti-kuste2860 and anti-kuste2861 antibodies, whereas no labelling was observed in the cytosol outside the membranous compartment (Fig. 3a). This confirmed a clear association of the hydrazine hydrolase with the anammoxosomes."

complete
CACAO 2363

9BACT:Q1Q0T3

part_of

GO:0044222: anammoxosome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

9BACT:Q1Q3H0

part_of

GO:0016469: proton-transporting two-sector ATPase complex

ECO:0000255: match to sequence model evidence used in manual assertion

C

Seeded From UniProt

Missing: with/from

9BACT:Q1Q3H0

GO:0016469: proton-transporting two-sector ATPase complex

ECO:0000255:

PMID:9254694[1]


C

Table 1.

complete
CACAO 2364

9BACT:Q1Q3H2

GO:0016469: proton-transporting two-sector ATPase complex

ECO:0000255:

PMID:9254694[1]


C

Table 1.

complete
CACAO 2365

9BACT:Q1Q3H2

part_of

GO:0016469: proton-transporting two-sector ATPase complex

ECO:0000255: match to sequence model evidence used in manual assertion

C

Seeded From UniProt

Missing: with/from


See also

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Altschul, SF et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 3389-402 PubMed GONUTS page