ID HZSA_KUEST Reviewed; 809 AA. AC Q1Q0T2; DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-SEP-2017, entry version 32. DE RecName: Full=Hydrazine synthase subunit alpha {ECO:0000303|PubMed:26479033}; DE Short=HZS-alpha {ECO:0000303|PubMed:26479033}; DE EC=1.7.2.7 {ECO:0000269|PubMed:21964329}; DE Flags: Precursor; GN ORFNames=kuste2861 {ECO:0000312|EMBL:CAJ73613.1}; OS Kuenenia stuttgartiensis. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Kuenenia. OX NCBI_TaxID=174633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16598256; DOI=10.1038/nature04647; RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., RA Taylor M.W., Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., RA Fonknechten N., Vallenet D., Segurens B., Schenowitz-Truong C., RA Medigue C., Collingro A., Snel B., Dutilh B.E., Op den Camp H.J., RA van der Drift C., Cirpus I., van de Pas-Schoonen K.T., Harhangi H.R., RA van Niftrik L., Schmid M., Keltjens J., van de Vossenberg J., RA Kartal B., Meier H., Frishman D., Huynen M.A., Mewes H., RA Weissenbach J., Jetten M.S.M., Wagner M., Le Paslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from RT a community genome."; RL Nature 440:790-794(2006). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PATHWAY, AND RP INDUCTION. RX PubMed=21964329; DOI=10.1038/nature10453; RA Kartal B., Maalcke W.J., de Almeida N.M., Cirpus I., Gloerich J., RA Geerts W., Op den Camp H.J., Harhangi H.R., Janssen-Megens E.M., RA Francoijs K.J., Stunnenberg H.G., Keltjens J.T., Jetten M.S., RA Strous M.; RT "Molecular mechanism of anaerobic ammonium oxidation."; RL Nature 479:127-130(2011). RN [3] {ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 28-809 IN COMPLEX WITH OTHER RP SUBUNITS OF THE HYDRAZINE SYNTHASE COMPLEX; ZINC AND HEMES, COFACTOR, RP FUNCTION, DOMAIN, AND REACTION MECHANISM. RX PubMed=26479033; DOI=10.1038/nature15517; RA Dietl A., Ferousi C., Maalcke W.J., Menzel A., de Vries S., RA Keltjens J.T., Jetten M.S., Kartal B., Barends T.R.; RT "The inner workings of the hydrazine synthase multiprotein complex."; RL Nature 527:394-397(2015). CC -!- FUNCTION: Component of the hydrazine synthase complex that CC catalyzes the condensation of nitric oxide (NO) with ammonium to CC form hydrazine (PubMed:21964329). The alpha subunit catalyzes the CC second half-reaction, i.e. the condensation of hydroxylamine CC formed in the active site of the gamma subunit with ammonia, CC yielding hydrazine (PubMed:26479033). Is involved in anaerobic CC ammonium oxidation (anammox), a biological process in which CC nitrite is used as the electron acceptor in the conversion of CC ammonium to dinitrogen gas (N2) and water; this bacterial process CC has a major role in the Earth's nitrogen cycle and has been CC estimated to synthesize up to 50% of the dinitrogen gas emitted CC into our atmosphere from the oceans (PubMed:21964329, CC PubMed:26479033). {ECO:0000269|PubMed:21964329, CC ECO:0000269|PubMed:26479033}. CC -!- CATALYTIC ACTIVITY: Hydrazine + H(2)O + 3 ferricytochrome c = CC nitric oxide + ammonium + 3 ferrocytochrome c. CC {ECO:0000269|PubMed:21964329}. CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000269|PubMed:26479033}; CC Note=Binds two heme c groups per subunit. CC {ECO:0000269|PubMed:26479033}; CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000269|PubMed:21964329}. CC -!- SUBUNIT: Part of the hydrazine synthase complex that forms an CC elongated dimer of heterotrimers composed of one alpha, one beta CC and one gamma subunit. {ECO:0000269|PubMed:26479033}. CC -!- SUBCELLULAR LOCATION: Anammoxosome {ECO:0000305|PubMed:21964329}. CC -!- INDUCTION: Is among the most highly expressed proteins in the CC proteome. {ECO:0000269|PubMed:21964329}. CC -!- DOMAIN: The alpha subunit consists of three domains: an N-terminal CC domain which includes a six-bladed beta-propeller, a middle domain CC binding a pentacoordinated c-type heme and a C-terminal domain CC which harbors a bis-histidine-coordinated c-type heme. CC {ECO:0000269|PubMed:26479033}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT573071; CAJ73613.1; -; Genomic_DNA. DR PDB; 5C2V; X-ray; 2.70 A; A/D=28-809. DR PDB; 5C2W; X-ray; 3.20 A; A/D=28-809. DR PDBsum; 5C2V; -. DR PDBsum; 5C2W; -. DR SMR; Q1Q0T2; -. DR DIP; DIP-61794N; -. DR KEGG; ag:CAJ73613; -. DR KO; K20934; -. DR BioCyc; MetaCyc:MONOMER-15348; -. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR009056; Cyt_c-like_dom. PE 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Signal; Zinc. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 809 Hydrazine synthase subunit alpha. FT /FTId=PRO_5004195495. FT DOMAIN 633 792 Cytochrome c. {ECO:0000255|PROSITE- FT ProRule:PRU00433}. FT METAL 303 303 Zinc. {ECO:0000269|PubMed:26479033}. FT METAL 587 587 Zinc; via tele nitrogen. FT {ECO:0000269|PubMed:26479033}. FT METAL 591 591 Iron (heme 1 axial ligand). FT {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. FT METAL 689 689 Iron (heme 2 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. FT METAL 772 772 Iron (heme 2 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. FT BINDING 583 583 Heme 1 (covalent). {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. FT BINDING 586 586 Heme 1 (covalent). {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. FT BINDING 685 685 Heme 2 (covalent). {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. FT BINDING 688 688 Heme 2 (covalent). {ECO:0000244|PDB:5C2V, FT ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033}. SQ SEQUENCE 809 AA; 90244 MW; 4D60D075EB87A7CF CRC64; MGKRKLGVIA SAFVAGALVC GSTLVNAEPV MTGGPVQGKA LWTDYSGMSK EVQGPVSQIL FTQSPRTAKG DPYQNYPHYI PEGSRIVLFD LNTKELKVLT NDFATAFDPC TYWDGKKFAF AGVHKKGGGC QIWEMNIDGS GLRQMTDLKG TCRSPIYYAA GSIEEGEGRI IWRDRYFEGD WKEHGMVEKT GMIIFSGSPE GVMDEFHNPY AYNLYRLDTQ GGKIIQRITG HVLSGIEFPH LNTTIDQITY NLSSNFDPWL TPDGNILFSS VQANGSRAGG EGRVMICVDN WDGAYPRPIY GNCDGEIGGT SGRSQAKITF GDRKIVYVES PYMNWGVGQL AAVSWDAPFN KTYEKLTGKD GGLYRSPYPL PDDRMLVSYA ERGDFGIYWF NFSKCAAGDK VYDDPNWNDH QPAPVYVKYK PRWINTFTAG KNFGVTVVTY QPFDQVKVEG YPHSWGTWIC FDTTLSDQPV GPYPHQKAKN VSHGDIKAVR IIQGYQCVEP DSTRFRVGAG AHLLGGERSS SNSGTAFQQR GIIGYQYVES DGSTVTSQLS DVPYYMQILD DKGMSVQTAL TWAYLRPYHG RICSGCHYGS YRGRAFKNIH AKALYNWWYD DRSHYDSPFA FRYLKFDNDG NYKGVKHGED VVVPSDIYYG GPSGTTSQPV EGLTLDKQRT VDFRRDIQPI LDAKCAMCHD SNNPPNLGGG LELVSVDGIA AYSRAYNSLL EPQRGKDPNI GGKYVNPSAA INSLLVWRLY EAELSANAPR EKIFPIEGRL LHNKFLTQDE RYAIVEWIDL GAQWDNIPGP DFYPGYLVK //