NOSZ_CUPNH
ID NOSZ_CUPNH Reviewed; 643 AA.
AC Q59105;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Nitrous-oxide reductase;
DE EC=1.7.2.4;
DE AltName: Full=N(2)OR;
DE AltName: Full=N2O reductase;
DE Flags: Precursor;
GN Name=nosZ; OrderedLocusNames=PHG252;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1324835; DOI=10.1111/j.1432-1033.1992.tb17156.x;
RA Zumft W.G., Dreusch A., Loechelt S., Cuypers H., Friedrich B.,
RA Schneider B.;
RT "Derived amino acid sequences of the nosZ gene (respiratory N2O reductase)
RT from Alcaligenes eutrophus, Pseudomonas aeruginosa and Pseudomonas stutzeri
RT reveal potential copper-binding residues. Implications for the CuA site of
RT N2O reductase and cytochrome-c oxidase.";
RL Eur. J. Biochem. 208:31-40(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
CC -!- FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory
CC system which is activated under anaerobic conditions in the presence of
CC nitrate or nitrous oxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c]
CC + 2 H(+) + nitrous oxide; Xref=Rhea:RHEA:43108, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17045, ChEBI:CHEBI:17997, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.7.2.4;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 6 Cu cations per subunit. Each subunit contains 2 copper
CC centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought
CC to be the site of nitrous oxide reduction. {ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the NosZ family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 2 family. {ECO:0000305}.
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DR EMBL; X65278; CAA46383.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP86001.1; -; Genomic_DNA.
DR PIR; S24382; S24382.
DR RefSeq; WP_011154164.1; NZ_CP039289.1.
DR AlphaFoldDB; Q59105; -.
DR SMR; Q59105; -.
DR STRING; 381666.PHG252; -.
DR EnsemblBacteria; AAP86001; AAP86001; PHG252.
DR GeneID; 39976708; -.
DR KEGG; reh:PHG252; -.
DR PATRIC; fig|381666.6.peg.200; -.
DR eggNOG; COG4263; Bacteria.
DR HOGENOM; CLU_016420_0_0_4; -.
DR OMA; HQEMQGY; -.
DR OrthoDB; 74414at2; -.
DR BioCyc; MetaCyc:MON-20927; -.
DR UniPathway; UPA00652; UER00709.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd04223; N2OR_C; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR HAMAP; MF_00716; NosZ; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR028096; EfeO_Cupredoxin.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR034205; N2OR_C.
DR InterPro; IPR023644; NO_Rdtase.
DR InterPro; IPR041114; Nos_propeller.
DR InterPro; IPR041142; NOS_propeller_2.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF13473; Cupredoxin_1; 1.
DR Pfam; PF18764; nos_propeller; 1.
DR Pfam; PF18793; nos_propeller_2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF50974; SSF50974; 1.
DR TIGRFAMs; TIGR04244; nitrous_NosZ_RR; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Calcium; Copper; Metal-binding; Oxidoreductase; Periplasm; Plasmid;
KW Reference proteome; Signal.
FT SIGNAL 1..46
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 47..643
FT /note="Nitrous-oxide reductase"
FT /id="PRO_0000019823"
FT REGION 548..643
FT /note="COX2-like"
FT BINDING 138
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 626
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 632
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 635
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 643 AA; 70085 MW; 42845B13497E4984 CRC64;
MSKEKASIGN GPGGIGRRQF LGTAALAGLA GVVACTDKGA APAAAAVGAP ASGAHGAAHG
AGASVHLKPG ELDTYYGLWS GGHTGDMRVL GLPSGREILR IPCFVPDALV GWGITNESKK
VMGARPDGTL RYTVADTHHT HASYKDGNYD GRYAWVNDKI NSRIARIRLD YFICDKITEL
PNVQGFHGIF PDKRDPVDTK INYTTRVFCG GEFGIPLPSA PTEDAGKYRS LFTCVDAETM
AVRWQVLIDG NCDLVATSYD GKLAATNQYN TENGAHFEDM MSAERDACVF FNIARIEAAV
QAGKFKTYGD SKVPVVDGTQ AANKDPKTAL TAYVSVPKNP HGVNASPDQK YFICAGKLSP
TATVIELSRV LGWFDGKQEK LDDAIVAEVE LGLGPLHTAF DGRGNAYTTL FLDSQLVKWN
LDAAIKFHKG DKNAKYVVDR LDLQYQPGHV NASQSETVAA DGKYLAVGCK FSKDRFLPVG
PLHPENEQLI DISGQKMVLM ADHPVRGEPH DFIIFKRELV RPKQVYALDD FPLAIKDPKE
SGVFRNGRKV TVKITSQAPA FSLREFKLKK GDEVTLILTN LDKIEDLTHG FAIPKYNVNF
IVNPQETASV TFVADKPGVF WCYCTHFCHA LHLEMRTRMI VEA
