NOSZ_BRADU
ID NOSZ_BRADU Reviewed; 650 AA.
AC Q89XJ6; O31382;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=blr0315;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RA Bedmar E.J., Velasco L., Xu C.A., Delgado M.J.;
RT "Bradyrhizobium japonicum nosRZDFYLX gene cluster.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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. {ECO:0000250}.
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; AJ002531; CAA05518.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC45580.1; -; Genomic_DNA.
DR PIR; T44660; T44660.
DR RefSeq; NP_766955.1; NC_004463.1.
DR RefSeq; WP_011083147.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89XJ6; -.
DR SMR; Q89XJ6; -.
DR STRING; 224911.27348563; -.
DR EnsemblBacteria; BAC45580; BAC45580; BAC45580.
DR GeneID; 64020174; -.
DR KEGG; bja:blr0315; -.
DR PATRIC; fig|224911.44.peg.8839; -.
DR eggNOG; COG4263; Bacteria.
DR HOGENOM; CLU_016420_0_0_5; -.
DR InParanoid; Q89XJ6; -.
DR OMA; HQEMQGY; -.
DR PhylomeDB; Q89XJ6; -.
DR BRENDA; 1.7.2.4; 14426.
DR UniPathway; UPA00652; UER00709.
DR Proteomes; UP000002526; Chromosome.
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 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; 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;
KW Reference proteome; Signal.
FT SIGNAL 1..46
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 47..650
FT /note="Nitrous-oxide reductase"
FT /id="PRO_0000019824"
FT REGION 552..650
FT /note="COX2-like"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT /evidence="ECO:0000250"
FT BINDING 593
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="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 630
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="A1"
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 636
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 639
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT CONFLICT 367
FT /note="D -> N (in Ref. 1; CAA05518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 71674 MW; 1B6C547D90501C5B CRC64;
MSDSDNIKGV SRRTLLGTTA AAAGVGLAGG AVVTKDGAGF VSTADAQTKS AAPKAPPARP
AVQKTEVAPG ELDEYYVFFS SGQSGEMRII GLPSMRELMR VPVFNRCSAT GWGQTNESLK
VLTEGMQPAT REFLKNRGGT FMNGDLHHPH VSFTDGTYDG RYAFMNDKAN SRVARVRLDV
MKCDKIIELP NQHTVHGLRL QKYPRTGYVF CNGEDGVPLP NDGKVLDNPK EYHSIFTALD
GDTMKVAWQV MVSGNLDNVD SDYQGKYCFS TCYNAEEGVT LAEMTANEQD WVVIFNLKRI
EEAVKKGDFK EMNGVPVIDG RKGSPYTRYV PVSNNPHGMN TAPDGIHIVA AGKLSPTVTV
MDVRLFDQLF DDKIKPRDVV VAEPELGLGP LHTAYDGKGN AYTTLFLDSQ VVKWNIDLAK
RAFKGEKVDP IIQKLDVHYQ PGHNHSSMGQ TKEADGKWLI SLNKFSKDRF LNVGPLKPEN
DQLIDISGDQ MKLVHDGPSF AEPHDATIVH RSKINPISIW DRADPMFADA VKQAKADGIN
LEADSKIIRD GNKVRVYMTS TAPAFGLEQF QVKQGDQVTV YITNIDAVED LTHGFCIVNY
GIQMEVAPMA TASVSFSADK AGVYWYYCSW FCHAMHMEMK GRMFVEPKSV
