HZSB_KUEST
ID HZSB_KUEST Reviewed; 386 AA.
AC Q1Q0T4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Hydrazine synthase subunit beta {ECO:0000303|PubMed:26479033};
DE Short=HZS-beta {ECO:0000303|PubMed:26479033};
DE Flags: Precursor;
GN ORFNames=kuste2859 {ECO:0000312|EMBL:CAJ73611.1};
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, 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 35-386 IN COMPLEX WITH OTHER
RP SUBUNITS OF THE HYDRAZINE SYNTHASE COMPLEX, FUNCTION, REACTION MECHANISM,
RP AND SUBUNIT.
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 beta subunit may play a role in modulating
CC transport of the hydroxylamine intermediate through a tunnel between
CC the gamma and alpha subunit's active site (PubMed:26479033). Is
CC involved in anaerobic ammonium oxidation (anammox), a biological
CC process in which nitrite is used as the electron acceptor in the
CC conversion of ammonium to dinitrogen gas (N2) and water; this bacterial
CC process 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 into
CC our atmosphere from the oceans (PubMed:21964329, PubMed:26479033).
CC {ECO:0000269|PubMed:21964329, 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}.
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DR EMBL; CT573071; CAJ73611.1; -; Genomic_DNA.
DR PDB; 5C2V; X-ray; 2.70 A; B/E=35-386.
DR PDB; 5C2W; X-ray; 3.20 A; B/E=35-386.
DR PDBsum; 5C2V; -.
DR PDBsum; 5C2W; -.
DR AlphaFoldDB; Q1Q0T4; -.
DR SMR; Q1Q0T4; -.
DR DIP; DIP-61792N; -.
DR IntAct; Q1Q0T4; 1.
DR KEGG; ag:CAJ73611; -.
DR BioCyc; MetaCyc:MON-15346; -.
DR GO; GO:0044222; C:anammoxosome; IDA:CACAO.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011964; YVTN_b-propeller_repeat.
DR SUPFAM; SSF50974; SSF50974; 1.
DR TIGRFAMs; TIGR02276; beta_rpt_yvtn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..386
FT /note="Hydrazine synthase subunit beta"
FT /id="PRO_0000441261"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 329..335
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:5C2V"
SQ SEQUENCE 386 AA; 41908 MW; B4C2BCC982852CD0 CRC64;
MVIRRKMNKM IRKGMIGAVM LGAAVAISGG VATAGYIQGT HVKTDLPGPF HITMSPDGST
LFISNQSGHS VTFVDARTQK VTGEVAVRVQ PEASAVTPDG AFLYVCNAES DSVSVVDIQR
KQEIKEIKVG DWPSGIKISP DGKTAYVACS GCMWNAIDVI DTGRMEKVRS IYTSDYGPRM
VEISPDGKTL VAILDTVGSI NRSVDFIDIA SGRVVENRVI HESSNLRDVV YTPDGKYIAV
THQTPKNWLP VCEAENGQVF TNNVTIIETK AGGKVARLPL DDLNNYDGNP YGMAMDPKGK
YLYIGVRGMH RVTILDMDKV LGLVRSSTQE ELDYLRDDLG LVRDYLVARV PTGLGPSSVC
LSPDGKFCYA ANYFSNNVTV IRTAVD
