HDH_KUEST
ID HDH_KUEST Reviewed; 582 AA.
AC Q1PW30;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Hydrazine dehydrogenase {ECO:0000303|PubMed:21964329};
DE Short=HDH {ECO:0000303|PubMed:21964329};
DE EC=1.7.2.8 {ECO:0000269|PubMed:21964329};
DE AltName: Full=Octaheme c-type cytochrome kustc0694 {ECO:0000303|PubMed:21964329};
DE Flags: Precursor;
GN ORFNames=kustc0694 {ECO:0000312|EMBL:CAJ71439.1};
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, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP 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]
RP REVIEW, FUNCTION, COFACTOR, AND TRANSLATIONAL START SITE.
RX PubMed=23210799; DOI=10.1111/1574-6976.12014;
RA Kartal B., de Almeida N.M., Maalcke W.J., Op den Camp H.J., Jetten M.S.,
RA Keltjens J.T.;
RT "How to make a living from anaerobic ammonium oxidation.";
RL FEMS Microbiol. Rev. 37:428-461(2013).
CC -!- FUNCTION: Catalyzes the four-electron oxidation of hydrazine to N2
CC (PubMed:21964329). The electrons derived from hydrazine oxidation may
CC be transferred to the quinone pool and exploited to promote the
CC generation of proton-motive force (pmf) across the anammoxosome
CC membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic
CC ammonium oxidation (anammox), a biological process in which nitrite is
CC used as the electron acceptor in the conversion of ammonium to
CC dinitrogen gas (N2) and water; this bacterial process has a major role
CC in the Earth's nitrogen cycle and has been estimated to synthesize up
CC to 50% of the dinitrogen gas emitted into our atmosphere from the
CC oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO
CC (PubMed:21964329). {ECO:0000269|PubMed:21964329,
CC ECO:0000303|PubMed:23210799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(III)-[cytochrome c] + hydrazine = 4 Fe(II)-[cytochrome c]
CC + 4 H(+) + N2; Xref=Rhea:RHEA:23232, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15571, ChEBI:CHEBI:17997,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.8;
CC Evidence={ECO:0000269|PubMed:21964329};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:Q50925};
CC Note=Binds 8 heme c groups per subunit. One of them is an atypical heme
CC c (unusual heme c binding motif CXXXXCH). Catalysis takes place at
CC heme-4, termed P460. The other c-type hemes mediate electron transfer
CC to the external electron acceptor, which is a cytochrome c-type
CC protein. {ECO:0000250|UniProtKB:Q50925, ECO:0000303|PubMed:23210799};
CC -!- ACTIVITY REGULATION: Is strongly and competitively inhibited by NO and
CC hydroxylamine. {ECO:0000269|PubMed:21964329}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000269|PubMed:21964329}.
CC -!- SUBCELLULAR LOCATION: Anammoxosome {ECO:0000305|PubMed:21964329}.
CC -!- INDUCTION: Is highly expressed (at protein level).
CC {ECO:0000269|PubMed:21964329}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ71439.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:23210799};
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DR EMBL; CT573073; CAJ71439.1; ALT_INIT; Genomic_DNA.
DR PDB; 6HIF; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-582.
DR PDBsum; 6HIF; -.
DR AlphaFoldDB; Q1PW30; -.
DR SMR; Q1PW30; -.
DR KEGG; ag:CAJ71439; -.
DR BioCyc; MetaCyc:MON-19883; -.
DR GO; GO:0044222; C:anammoxosome; IDA:CACAO.
DR GO; GO:0033740; F:hydroxylamine oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..582
FT /note="Hydrazine dehydrogenase"
FT /id="PRO_0000441263"
FT REGION 561..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 124
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 125
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:0000250|UniProtKB:Q50925"
FT BINDING 141
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 151
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 154
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 155
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:0000250|UniProtKB:Q50925"
FT BINDING 159
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:0000250|UniProtKB:Q50925, ECO:0000305"
FT BINDING 170
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 175
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925,
FT ECO:0000305|PubMed:23210799"
FT BINDING 176
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925,
FT ECO:0000305|PubMed:23210799"
FT BINDING 191
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 216
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 219
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 220
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 227
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 230
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 231
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 234
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:0000250|UniProtKB:Q50925"
FT BINDING 247
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 250
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 251
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 267
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 297
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 300
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 301
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 306
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 342
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 345
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 346
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 454
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
SQ SEQUENCE 582 AA; 65577 MW; 3006EE78AC726B96 CRC64;
MRKFLKVTLA SALIGCGVIG TVSSLMVKEA KAVEIITHWV PHEVYGMPGE PDNSGKVFFS
GLKAKYMGYP KDAQRSPYPG KYSKFWKTLP AYRYYIPDYM YNRDEVRPSN PIKGTFKLEQ
CVACHSVMTP GIVRDYNKSA HSKAEPAPTG CDTCHGNNHQ KLTMPSSKAC GTAECHETQY
NEQGQGGIGS HASCSSFAQV ECAWSIERPP GDTAGCTFCH TSPEERCSTC HQRHQFDPAV
ARRSEQCKTC HWGKDHRDWE AYDIGLHGTV YQVNKWDTEQ FDFSKKLSDA DYVGPTCQYC
HMRGGHHNVQ RASIVYTSMG MSMADRGAPL WKEKRDRWVS ICDDCHSPRF ARENLQAMDE
SVKDASLKYR ETFKVAEDLL IDGVLDPMPK DLCPDWSGQH IWSLKIGAYH DGEAYGGTTG
ESGEFRMSNC TDVERLCFES VGYFQTYIYK GMAHGSWNDA TYSDGSFGMD RWLVNVKQNA
SRARRLAALE KKVGISWQPE QFWKTGEWLD QLTGPYIVKN HPGKTIFDLC PDPGWLDTHH
APAEEVEYIE RKLKELGITA GSHSAHHHES GHDPAARSMK EH
