NRHAO_KUEST
ID NRHAO_KUEST Reviewed; 852 AA.
AC P0DV45;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Probable nitrite reductase-hydroxylamine oxidoreductase fusion protein {ECO:0000303|PubMed:28263314};
DE Short=NIR-HAO {ECO:0000303|PubMed:28263314};
DE EC=1.7.2.1 {ECO:0000250|UniProtKB:Q02219};
DE EC=1.7.2.6 {ECO:0000250|UniProtKB:Q50925};
DE Flags: Precursor;
OS Kuenenia stuttgartiensis.
OC Bacteria; Planctomycetes; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Kuenenia.
OX NCBI_TaxID=174633;
RN [1] {ECO:0000312|EMBL:CAJ73226.1}
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, AND SUBCELLULAR LOCATION.
RX PubMed=28263314; DOI=10.1038/nmicrobiol.2017.29;
RA Giessen T.W., Silver P.A.;
RT "Widespread distribution of encapsulin nanocompartments reveals functional
RT diversity.";
RL Nat. Microbiol. 2:17029-17029(2017).
CC -!- FUNCTION: A nitrite reductase-hydroxylamine oxidoreductase protein that
CC probably functions in the type 1 encapsulin nanocompartment. Probably
CC involved in reductive catalysis. Targeted to the encapsulin
CC nanocompartment by association with the diheme domain of the encapsulin
CC shell protein (AC Q1Q6L7) (Probable). Catalyzes the reduction of
CC nitrite to nitric oxide (NO) (By similarity). Catalyzes the oxidation
CC of hydroxylamine to nitrite (By similarity).
CC {ECO:0000250|UniProtKB:Q02219, ECO:0000250|UniProtKB:Q50925,
CC ECO:0000305|PubMed:28263314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(III)-[cytochrome c] + H2O + hydroxylamine = 4 Fe(II)-
CC [cytochrome c] + 5 H(+) + nitrite; Xref=Rhea:RHEA:45032, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q50925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-
CC [cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.1;
CC Evidence={ECO:0000250|UniProtKB:Q02219};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q02219};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 8 heme groups per subunit. {ECO:0000250|UniProtKB:Q50925};
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:28263314}.
CC -!- MISCELLANEOUS: In (PubMed:28263314) the construct expressed
CC anaerobically in E.coli contains only the nitrite reductase domain
CC (residues 28-327). {ECO:0000269|PubMed:28263314}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the multicopper
CC oxidase family. {ECO:0000305}.
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; CAJ73226.1; -; Genomic_DNA.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR SUPFAM; SSF49503; SSF49503; 2.
PE 3: Inferred from homology;
KW Copper; Encapsulin nanocompartment; Heme; Iron; Metal-binding;
KW Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..852
FT /note="Probable nitrite reductase-hydroxylamine
FT oxidoreductase fusion protein"
FT /id="PRO_0000455329"
FT DOMAIN 72..169
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 217..307
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT REGION 28..327
FT /note="Nitrite reductase domain"
FT /evidence="ECO:0000305|PubMed:28263314"
FT REGION 328..827
FT /note="Hydroxylamine oxidoreductase domain"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:Q02219"
FT BINDING 145
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:Q02219"
FT BINDING 406
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 409
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 410
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:0000250|UniProtKB:Q50925"
FT BINDING 426
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 463
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 466
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 467
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:0000250|UniProtKB:Q50925"
FT BINDING 471
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:0000250|UniProtKB:Q50925"
FT BINDING 483
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 486
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 487
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 505
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 537
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 543
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 546
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 547
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 550
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:0000250|UniProtKB:Q50925"
FT BINDING 563
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 566
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 567
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 614
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 617
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 618
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 686
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 689
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q50925"
FT BINDING 690
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 813
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 852 AA; 96352 MW; C8E27B60047708A6 CRC64;
MLNKSAALVP VVLAFLFLFL CFQCLYADIR CLTGKDGAVH LEMEAKPLTI EPRPGVFFDA
WGYCLKGDVP TVPGPVIKVR EGTKVKILFR NKLTVPASIH PHGVKYTTAN VGVNIAGNPA
SIVAPGDSRI FEWDTAGTPG TWFYHSYVFE RGGEEGLSRG LWGALIVEPV GGDPNPPDKE
FVVFMHAFNV NGQEYYAFNN KSGDIELMRG DSSAFPGETW KAKMGDKVRF HLINITEEAH
TFHTHGHRWL DKSCDKLIDT IGLNPFDSYV LDFVAGEGVG KGNWAFHCQS QEHMMNGMFG
IFMVEEGKRV NAVIASCDEG RKTLSAPGQD RQPPTLEGFS GAYMYPEITE KNMYESFAGL
EKGDGIWGDY YSPIPLYTYF NPSRHYVPPE SDAYTNLLVK YRPDQCVECH EETTPGIVAE
WKMSNHANPK KNPHVSAETQ EIEALIGKEL NNWRPGTKDG VYCSYCHGSD HEKLFMPTVD
NSCGACHPKQ AAEFIKGRDH GRPNHPQSWE GNVSTPWYAE YYRRGEGYSM VGCDQCHQNM
SSCDDCHSRH RFSAAEARRP EACSICHMGP DHPDWESYSR SKWGVIYETT KERWNWDKNL
AEVIPGEDYL APTCQYCHMY VGNNKWEMNV ETKGIWRMGV IPPKEVEFKS GLKDFPYGIK
IPPMDKKLEI YSAESQEKRR KWVELCSKCH SSRFAGMWLD SLDQYMFESW RRIDEAQLII
EKLFSENAIE PPPEKRPPFP LSDLIIKVLG AEKLGAEMYR LFKQTNGHLP VIGPILGAYS
IFTQNEGNPG GIEREYAEMW FWSHLQGYKG AAHAQPDISW WWGTAQGVGN LTRIRDEAEK
LRRLKSGSSS GF
