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NOSZ_BRUSU
ID   NOSZ_BRUSU              Reviewed;         639 AA.
AC   Q8FX16; G0KFB0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=BRA0275, BS1330_II0272;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014292; AAN33476.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM19754.1; -; Genomic_DNA.
DR   RefSeq; WP_002967358.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FX16; -.
DR   SMR; Q8FX16; -.
DR   PRIDE; Q8FX16; -.
DR   EnsemblBacteria; AEM19754; AEM19754; BS1330_II0272.
DR   GeneID; 45053343; -.
DR   KEGG; bms:BRA0275; -.
DR   KEGG; bsi:BS1330_II0272; -.
DR   PATRIC; fig|204722.22.peg.3061; -.
DR   HOGENOM; CLU_016420_0_0_5; -.
DR   OMA; HQEMQGY; -.
DR   PhylomeDB; Q8FX16; -.
DR   UniPathway; UPA00652; UER00709.
DR   Proteomes; UP000007104; 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_0000019826"
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;  71071 MW;  DFB2E8DBB372B057 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 APDGIHVVAN 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
 
 
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