HZSA_KUEST
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 03-AUG-2022, entry version 47.
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 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 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 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.
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}.
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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 AlphaFoldDB; Q1Q0T2; -.
DR SMR; Q1Q0T2; -.
DR DIP; DIP-61794N; -.
DR IntAct; Q1Q0T2; 2.
DR KEGG; ag:CAJ73613; -.
DR BioCyc; MetaCyc:MON-15348; -.
DR BRENDA; 1.7.2.7; 11008.
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 BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:26479033"
FT BINDING 583
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 586
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 587
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:26479033"
FT BINDING 591
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 685
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 688
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26479033,
FT ECO:0007744|PDB:5C2V, ECO:0007744|PDB:5C2W"
FT BINDING 689
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 772
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 30..32
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 275..281
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5C2W"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 405..414
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 445..449
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 508..512
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 580..589
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 602..606
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 673..676
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 677..684
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 685..688
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 714..719
FT /evidence="ECO:0007829|PDB:5C2V"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 744..749
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 766..768
FT /evidence="ECO:0007829|PDB:5C2V"
FT HELIX 778..789
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:5C2V"
FT STRAND 802..804
FT /evidence="ECO:0007829|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
