Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329). The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO (PubMed:21964329). 4 Fe(III)-[cytochrome c] + hydrazine = 4 Fe(II)-[cytochrome c] + 4 H(+) + N2 Binds 8 heme c groups per subunit. One of them is an atypical heme c (unusual heme c binding motif CXXXXCH). Catalysis takes place at heme-4, termed P460. The other c-type hemes mediate electron transfer to the external electron acceptor, which is a cytochrome c-type protein. Is strongly and competitively inhibited by NO and hydroxylamine. Nitrogen metabolism. Is highly expressed (at protein level). Extended N-terminus.