NOSZ_BRUME
ID NOSZ_BRUME Reviewed; 639 AA.
AC Q8YBC6; Q8YBC7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
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=BMEII0973/BMEII0974;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL54215.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL54216.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008918; AAL54215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE008918; AAL54216.1; ALT_SEQ; Genomic_DNA.
DR PIR; AD3631; AD3631.
DR PIR; AE3631; AE3631.
DR AlphaFoldDB; Q8YBC6; -.
DR SMR; Q8YBC6; -.
DR STRING; 224914.BMEII0973; -.
DR EnsemblBacteria; AAL54215; AAL54215; BMEII0973.
DR EnsemblBacteria; AAL54216; AAL54216; BMEII0974.
DR KEGG; bme:BMEII0973; -.
DR KEGG; bme:BMEII0974; -.
DR eggNOG; COG4263; Bacteria.
DR OMA; HQEMQGY; -.
DR UniPathway; UPA00652; UER00709.
DR Proteomes; UP000000419; Chromosome II.
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; 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; PF00116; COX2; 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; Signal.
FT SIGNAL 1..44
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 45..639
FT /note="Nitrous-oxide reductase"
FT /id="PRO_0000019825"
FT REGION 541..639
FT /note="COX2-like"
FT BINDING 136
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT /evidence="ECO:0000250"
FT BINDING 582
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 617
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 617
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 621
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 621
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 625
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"
SQ SEQUENCE 639 AA; 71087 MW; CFF2E492E332B54E CRC64;
MTEETRKSQL SRRQLLGTSA FVAAAGASGL GGALLAGSSE TALAAGAAKG GMSPEVKPGE
LDEYYVFFSS GQCGEVRIVG LPSMRELMRI PVFNRDSATG WGLTNESRKV LTEGLLPQDR
EFLKDRGDIF LNGDLHHPHP SFTDGTYDGR YLYANDKANT RVCRIRLDVM KCDKIIQLPN
QHTVHGLRVQ KYPKTGYVFC NGEDRVPIPN DGSHLNDVKQ YHAIFTAVDG ETMKVAWQVM
VDGNLDNVDC DYQGKYAFST CYNSEEGTTL AEMMSSEQDW IVVFNLKRIE EAVANGDFKE
MNGVPVIDGR HGSKYTRYIP VPNSPHGINT ALDGIHVVAN GKLSPTVTVF DVRKFDDLFD
DKIKPRDAVV AEPELGLGPL HTAYDDKGNA YTTLFIDSQI CKWNIEDAKR AFKGEKVDPI
RQKLDVHYQP GHNHSSMGQT KEVDGKWLIS LNKFSKDRYL NVGPLKPEND QLIDISGDKM
VIVHDGPSFA EPHDATIVHR SKINPVSFWS REDPFFADAV AQAKADGLDL MEANEVVRDG
NKVRVYMTSS APAFGLTEFT VQQDDEVTVY VTNIDEIEDL THGFAIVNYG VNMEVAPQAT
ASVTFKASKP GVWWYYCSWF CHAMHMEMQG RMLVEPKKA
