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NOSZ_RHIME
ID   NOSZ_RHIME              Reviewed;         639 AA.
AC   Q59746;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 135.
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=RA0643; ORFNames=SMa1182;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JJ1c10;
RX   PubMed=8626275; DOI=10.1128/jb.178.6.1505-1514.1996;
RA   Holloway P., McCormick W., Watson R.J., Chan Y.K.;
RT   "Identification and analysis of the dissimilatory nitrous oxide reduction
RT   genes, nosRZDFY, of Rhizobium meliloti.";
RL   J. Bacteriol. 178:1505-1514(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; U47133; AAC44023.1; -; Genomic_DNA.
DR   EMBL; AE006469; AAK65301.1; -; Genomic_DNA.
DR   PIR; C95342; C95342.
DR   RefSeq; NP_435889.1; NC_003037.1.
DR   RefSeq; WP_010967622.1; NC_003037.1.
DR   AlphaFoldDB; Q59746; -.
DR   SMR; Q59746; -.
DR   EnsemblBacteria; AAK65301; AAK65301; SMa1182.
DR   GeneID; 61599412; -.
DR   KEGG; sme:SMa1182; -.
DR   PATRIC; fig|266834.11.peg.663; -.
DR   HOGENOM; CLU_016420_0_0_5; -.
DR   OMA; HQEMQGY; -.
DR   UniPathway; UPA00652; UER00709.
DR   Proteomes; UP000001976; Plasmid pSymA.
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..639
FT                   /note="Nitrous-oxide reductase"
FT                   /id="PRO_0000019833"
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;  70760 MW;  EBCF5EDFAFF70B96 CRC64;
     MSNEETKMRL NRRQMLGTTA FMAAAGAVGA GGALTLSGGT ATPARAQETS GSSYEVKPGE
     LDEYYVFFSS GQSGEIRIVG APSMREMMRI PVFNRCSATG WGQTNESRKV MTEGLLPETV
     EFLKDQGGLY LNGDLHHPHP SFTDGTYDGR YLYANDKSNS RVCRIRLDVM KCDKIIQLPN
     QHTVHGLRVQ KYPKTGYVFC NGEDAVPVPN DGKTMGDKNS YQAIFTAVDG ETMEVAWQVM
     VDGNLDNVDA DYQGKYCFAT CYNSEEGFTL ADMMASEQDW VVIFNLKRIE EAVAKGDYKE
     IGGVPVLDGR KGSPYTRYVP VPNSPHGINT APDGIHVVAN GKLSPTVTVF DVRKFDDLFD
     DKIQARDTVV AEPELGLGPL HTAYDGKGNA YTTLFIDSQV CKWNIEDAKR AYAGEKVDPI
     RHKLDVHYQP GHNHTSMGQT KEADGKWLIS LNKFSKDRYL NVGPLKPEND QLIDISGDEM
     VLVHDNPTFA EPHDATIVHA SKINPVHVWN RDDPFFADAV AQAKADNIDL MVDSEVIRDG
     NKVRVYMTSA APAFGLDDFT VKQGDEVTVY VTNIDEVEDL THGFCIVNYG INMEVAPQAT
     ASVTFKASRP GVYWYYCTWF CHAMHMEMKG RMLVEAQGA
 
 
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