HZSG_KUEST
ID HZSG_KUEST Reviewed; 353 AA.
AC Q1Q0T3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Hydrazine synthase subunit gamma {ECO:0000303|PubMed:26479033};
DE Short=HZS-gamma {ECO:0000303|PubMed:26479033};
DE EC=1.7.2.7 {ECO:0000269|PubMed:21964329};
DE Flags: Precursor;
GN ORFNames=kuste2860 {ECO:0000312|EMBL:CAJ73612.1};
OS Kuenenia stuttgartiensis.
OC Bacteria; Planctomycetes; Candidatus Brocadiia; 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:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 40-353 IN COMPLEX WITH OTHER
RP SUBUNITS OF THE HYDRAZINE SYNTHASE COMPLEX; HEMES AND CALCIUM IONS,
RP COFACTOR, 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 gamma subunit catalyzes the first half-reaction,
CC i.e. the three-electron reduction of nitric oxide to hydroxylamine; it
CC may obtain electrons from the triheme cytochrome c kuste2854
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 Fe(II)-
CC [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. Heme 1 appears to be in the
CC active site, whereas heme 2 probably functions in electron transfer.
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: Consists of two alpha-helical lobes, each of which contains one
CC c-type heme. {ECO:0000269|PubMed:26479033}.
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DR EMBL; CT573071; CAJ73612.1; -; Genomic_DNA.
DR PDB; 5C2V; X-ray; 2.70 A; C/F=40-353.
DR PDB; 5C2W; X-ray; 3.20 A; C/F=40-353.
DR PDBsum; 5C2V; -.
DR PDBsum; 5C2W; -.
DR AlphaFoldDB; Q1Q0T3; -.
DR SMR; Q1Q0T3; -.
DR DIP; DIP-61793N; -.
DR IntAct; Q1Q0T3; 1.
DR KEGG; ag:CAJ73612; -.
DR BioCyc; MetaCyc:MON-15347; -.
DR GO; GO:0044222; C:anammoxosome; IDA:CACAO.
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; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Heme; Iron; Metal-binding; Oxidoreductase; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..353
FT /note="Hydrazine synthase subunit gamma"
FT /id="PRO_0000441262"
FT DOMAIN 209..353
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 102
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 105
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 106
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 165
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 225
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 228
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 229
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 332
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:5C2V"
SQ SEQUENCE 353 AA; 38925 MW; 342EA10F32D59E37 CRC64;
MAREMRLGGK ERMKTGVVKI GLVAALGVVG LISAGGVYAG QPRVISTIQT GATWEPLGRE
EPLTVPEVHF RVKHSPFKSE LVRYGQFQFN DAAWSLQGSY SCASCHYERG QTTGLIWDLG
DEGWGSWKNT KYIRGGRYLP PFRHEGFTGH PDEIVGATSS LDRVCGRDPG FVFRSENFSP
MRLEALICYI RALEFTGSPF RNADGSLTEA QKRGQKIFED PKVGCLECHP GDPMDPRALF
SDAQTHDVGT GRVGVNGFRS TPGKVFNISA LEAGEDPYGV ESNTPIIGLD LVKEFDTPTL
RDIYASGTYF HDGGARTLMD TINNTVNDKD MHGRTSHLKQ QELQDLVEYL KAL
