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 28-FEB-2018, entry version 35. 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 IntAct; Q1Q0T2; 2. DR KEGG; ag:CAJ73613; -. DR KO; K20934; -. DR BioCyc; MetaCyc:MONOMER-15348; -. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.120.10.30; -; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. 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}. FT STRAND 30 32 {ECO:0000244|PDB:5C2V}. FT HELIX 45 52 {ECO:0000244|PDB:5C2V}. FT STRAND 58 67 {ECO:0000244|PDB:5C2V}. FT TURN 68 70 {ECO:0000244|PDB:5C2V}. FT HELIX 73 75 {ECO:0000244|PDB:5C2V}. FT STRAND 85 90 {ECO:0000244|PDB:5C2V}. FT TURN 91 93 {ECO:0000244|PDB:5C2V}. FT STRAND 96 99 {ECO:0000244|PDB:5C2V}. FT STRAND 103 111 {ECO:0000244|PDB:5C2V}. FT STRAND 113 124 {ECO:0000244|PDB:5C2V}. FT STRAND 127 136 {ECO:0000244|PDB:5C2V}. FT STRAND 149 158 {ECO:0000244|PDB:5C2V}. FT STRAND 163 173 {ECO:0000244|PDB:5C2V}. FT STRAND 181 188 {ECO:0000244|PDB:5C2V}. FT STRAND 192 201 {ECO:0000244|PDB:5C2V}. FT STRAND 213 218 {ECO:0000244|PDB:5C2V}. FT HELIX 223 228 {ECO:0000244|PDB:5C2V}. FT STRAND 234 238 {ECO:0000244|PDB:5C2V}. FT TURN 239 242 {ECO:0000244|PDB:5C2V}. FT STRAND 243 247 {ECO:0000244|PDB:5C2V}. FT STRAND 255 260 {ECO:0000244|PDB:5C2V}. FT STRAND 266 272 {ECO:0000244|PDB:5C2V}. FT TURN 275 281 {ECO:0000244|PDB:5C2V}. FT STRAND 283 289 {ECO:0000244|PDB:5C2V}. FT STRAND 297 303 {ECO:0000244|PDB:5C2V}. FT STRAND 312 318 {ECO:0000244|PDB:5C2V}. FT STRAND 320 322 {ECO:0000244|PDB:5C2V}. FT STRAND 324 332 {ECO:0000244|PDB:5C2V}. FT STRAND 338 347 {ECO:0000244|PDB:5C2V}. FT HELIX 350 352 {ECO:0000244|PDB:5C2V}. FT STRAND 354 357 {ECO:0000244|PDB:5C2V}. FT STRAND 359 361 {ECO:0000244|PDB:5C2W}. FT STRAND 363 369 {ECO:0000244|PDB:5C2V}. FT STRAND 375 383 {ECO:0000244|PDB:5C2V}. FT STRAND 385 391 {ECO:0000244|PDB:5C2V}. FT TURN 392 395 {ECO:0000244|PDB:5C2V}. FT STRAND 396 402 {ECO:0000244|PDB:5C2V}. FT STRAND 405 414 {ECO:0000244|PDB:5C2V}. FT STRAND 427 430 {ECO:0000244|PDB:5C2V}. FT STRAND 433 435 {ECO:0000244|PDB:5C2V}. FT STRAND 437 439 {ECO:0000244|PDB:5C2V}. FT STRAND 442 444 {ECO:0000244|PDB:5C2V}. FT TURN 445 449 {ECO:0000244|PDB:5C2V}. FT STRAND 455 461 {ECO:0000244|PDB:5C2V}. FT STRAND 476 479 {ECO:0000244|PDB:5C2V}. FT TURN 483 485 {ECO:0000244|PDB:5C2V}. FT STRAND 488 494 {ECO:0000244|PDB:5C2V}. FT STRAND 502 504 {ECO:0000244|PDB:5C2V}. FT TURN 508 512 {ECO:0000244|PDB:5C2V}. FT HELIX 516 518 {ECO:0000244|PDB:5C2V}. FT STRAND 520 522 {ECO:0000244|PDB:5C2V}. FT STRAND 524 526 {ECO:0000244|PDB:5C2V}. FT STRAND 530 537 {ECO:0000244|PDB:5C2V}. FT STRAND 544 552 {ECO:0000244|PDB:5C2V}. FT STRAND 554 559 {ECO:0000244|PDB:5C2V}. FT STRAND 565 568 {ECO:0000244|PDB:5C2V}. FT STRAND 580 589 {ECO:0000244|PDB:5C2V}. FT TURN 590 593 {ECO:0000244|PDB:5C2V}. FT HELIX 602 606 {ECO:0000244|PDB:5C2V}. FT STRAND 621 626 {ECO:0000244|PDB:5C2V}. FT STRAND 628 630 {ECO:0000244|PDB:5C2V}. FT STRAND 632 636 {ECO:0000244|PDB:5C2V}. FT HELIX 665 667 {ECO:0000244|PDB:5C2V}. FT TURN 673 676 {ECO:0000244|PDB:5C2V}. FT HELIX 677 684 {ECO:0000244|PDB:5C2V}. FT TURN 685 688 {ECO:0000244|PDB:5C2V}. FT STRAND 693 695 {ECO:0000244|PDB:5C2V}. FT HELIX 714 719 {ECO:0000244|PDB:5C2V}. FT TURN 728 730 {ECO:0000244|PDB:5C2V}. FT HELIX 744 749 {ECO:0000244|PDB:5C2V}. FT STRAND 755 757 {ECO:0000244|PDB:5C2V}. FT STRAND 759 761 {ECO:0000244|PDB:5C2V}. FT STRAND 766 768 {ECO:0000244|PDB:5C2V}. FT HELIX 778 789 {ECO:0000244|PDB:5C2V}. FT STRAND 797 800 {ECO:0000244|PDB:5C2V}. FT STRAND 802 804 {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 //