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 02-DEC-2020, entry version 42. 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; Candidatus Brocadiae; 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., Taylor M.W., RA Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N., RA Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A., RA Snel B., Dutilh B.E., Op den Camp H.J., van der Drift C., Cirpus I., RA van de Pas-Schoonen K.T., Harhangi H.R., van Niftrik L., Schmid M., RA Keltjens J., van de Vossenberg J., Kartal B., Meier H., Frishman D., RA Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M., RA Le Paslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from a RT community genome."; RL Nature 440:790-794(2006). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PATHWAY, AND 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., 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., Keltjens J.T., RA 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 catalyzes CC the condensation of nitric oxide (NO) with ammonium to form hydrazine CC (PubMed:21964329). The alpha subunit catalyzes the second half- CC reaction, i.e. the condensation of hydroxylamine formed in the active CC site of the gamma subunit with ammonia, yielding hydrazine CC (PubMed:26479033). Is involved in anaerobic ammonium oxidation CC (anammox), a biological process in which nitrite is used as the CC electron acceptor in the conversion of ammonium to dinitrogen gas (N2) CC and water; this bacterial process has a major role in the Earth's CC nitrogen cycle and has been estimated to synthesize up to 50% of the CC dinitrogen gas emitted into our atmosphere from the oceans CC (PubMed:21964329, PubMed:26479033). {ECO:0000269|PubMed:21964329, CC ECO:0000269|PubMed:26479033}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3 [Fe(III)cytochrome c] + H2O + hydrazine = 3 CC [Fe(II)cytochrome c] + 2 H(+) + NH4(+) + nitric oxide; CC Xref=Rhea:RHEA:49816, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15571, CC ChEBI:CHEBI:16480, ChEBI:CHEBI:28938, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=1.7.2.7; CC Evidence={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 elongated CC dimer of heterotrimers composed of one alpha, one beta and one gamma CC subunit. {ECO:0000269|PubMed:26479033}. CC -!- SUBCELLULAR LOCATION: Anammoxosome {ECO:0000305|PubMed:21964329}. CC -!- INDUCTION: Is among the most highly expressed proteins in the proteome. CC {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 which CC 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 IntAct; Q1Q0T2; 2. DR KEGG; ag:CAJ73613; -. DR BioCyc; MetaCyc:MONOMER-15348; -. DR GO; GO:0044222; C:anammoxosome; IDA:CACAO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 2.120.10.30; -; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR040698; HZS_alpha_mid. DR Pfam; PF18582; HZS_alpha; 1. PE 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Signal; Zinc. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..809 FT /note="Hydrazine synthase subunit alpha" FT /id="PRO_5004195495" FT DOMAIN 633..792 FT /note="Cytochrome c" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT METAL 303 FT /note="Zinc" FT /evidence="ECO:0000269|PubMed:26479033" FT METAL 587 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000269|PubMed:26479033" FT METAL 591 FT /note="Iron (heme 1 axial ligand)" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT METAL 689 FT /note="Iron (heme 2 axial ligand); via tele nitrogen" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT METAL 772 FT /note="Iron (heme 2 axial ligand); via tele nitrogen" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT BINDING 583 FT /note="Heme 1 (covalent)" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT BINDING 586 FT /note="Heme 1 (covalent)" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT BINDING 685 FT /note="Heme 2 (covalent)" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT BINDING 688 FT /note="Heme 2 (covalent)" FT /evidence="ECO:0000244|PDB:5C2V, ECO:0000244|PDB:5C2W, FT ECO:0000269|PubMed:26479033" FT STRAND 30..32 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 45..52 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 58..67 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 68..70 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 73..75 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 85..90 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 91..93 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 96..99 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 103..111 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 113..124 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 127..136 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 149..158 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 163..173 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 181..188 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 192..201 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 213..218 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 223..228 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 234..238 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 239..242 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 243..247 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 255..260 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 266..272 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 275..281 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 283..289 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 297..303 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 312..318 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 320..322 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 324..332 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 338..347 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 350..352 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 354..357 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 359..361 FT /evidence="ECO:0000244|PDB:5C2W" FT STRAND 363..369 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 375..383 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 385..391 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 392..395 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 396..402 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 405..414 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 427..430 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 433..435 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 437..439 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 442..444 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 445..449 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 455..461 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 476..479 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 483..485 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 488..494 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 502..504 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 508..512 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 516..518 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 520..522 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 524..526 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 530..537 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 544..552 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 554..559 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 565..568 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 580..589 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 590..593 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 602..606 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 621..626 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 628..630 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 632..636 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 665..667 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 673..676 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 677..684 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 685..688 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 693..695 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 714..719 FT /evidence="ECO:0000244|PDB:5C2V" FT TURN 728..730 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 744..749 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 755..757 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 759..761 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 766..768 FT /evidence="ECO:0000244|PDB:5C2V" FT HELIX 778..789 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 797..800 FT /evidence="ECO:0000244|PDB:5C2V" FT STRAND 802..804 FT /evidence="ECO:0000244|PDB:5C2V" 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 //