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Nitrous-oxide reductase (EC 1.7.2.4) (N(2)OR) (N2O reductase)

 A0A165T1D8_9RHOB        Unreviewed;       645 AA.
A0A165T1D8;
06-JUL-2016, integrated into UniProtKB/TrEMBL.
06-JUL-2016, sequence version 1.
25-APR-2018, entry version 8.
RecName: Full=Nitrous-oxide reductase {ECO:0000256|HAMAP-Rule:MF_00716};
EC=1.7.2.4 {ECO:0000256|HAMAP-Rule:MF_00716};
AltName: Full=N(2)OR {ECO:0000256|HAMAP-Rule:MF_00716};
AltName: Full=N2O reductase {ECO:0000256|HAMAP-Rule:MF_00716};
Name=nosZ {ECO:0000256|HAMAP-Rule:MF_00716,
ECO:0000313|EMBL:KZL05162.1};
ORFNames=PsAD2_04517 {ECO:0000313|EMBL:KZL05162.1};
Pseudovibrio axinellae.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Pseudovibrio.
NCBI_TaxID=989403 {ECO:0000313|EMBL:KZL05162.1, ECO:0000313|Proteomes:UP000076577};
[1] {ECO:0000313|EMBL:KZL05162.1, ECO:0000313|Proteomes:UP000076577}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ad2 {ECO:0000313|EMBL:KZL05162.1,
ECO:0000313|Proteomes:UP000076577};
PubMed=27065959; DOI=10.3389/fmicb.2016.00387;
Romano S., Fernandez-Guerra A., Reen F.J., Glockner F.O.,
Crowley S.P., O'Sullivan O., Cotter P.D., Adams C., Dobson A.D.,
O'Gara F.;
"Comparative Genomic Analysis Reveals a Diverse Repertoire of Genes
Involved in Prokaryote-Eukaryote Interactions within the Pseudovibrio
Genus.";
Front. Microbiol. 7:387-387(2016).
-!- FUNCTION: Nitrous-oxide reductase is part of a bacterial
respiratory system which is activated under anaerobic conditions
in the presence of nitrate or nitrous oxide. {ECO:0000256|HAMAP-
Rule:MF_00716}.
-!- CATALYTIC ACTIVITY: Nitrogen + H(2)O + 2 ferricytochrome c =
nitrous oxide + 2 ferrocytochrome c + 2 H(+). {ECO:0000256|HAMAP-
Rule:MF_00716}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000256|HAMAP-Rule:MF_00716};
Note=Binds 2 calcium ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_00716};
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000256|HAMAP-Rule:MF_00716};
Note=Binds 6 Cu cations per subunit. Each subunit contains 2
copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z)
is thought to be the site of nitrous oxide reduction.
{ECO:0000256|HAMAP-Rule:MF_00716};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00716}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_00716}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
{ECO:0000256|HAMAP-Rule:MF_00716}.
-!- SIMILARITY: Belongs to the NosZ family. {ECO:0000256|HAMAP-
Rule:MF_00716}.
-!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
oxidase subunit 2 family. {ECO:0000256|HAMAP-Rule:MF_00716}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KZL05162.1}.
-----------------------------------------------------------------------
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EMBL; LMCB01000159; KZL05162.1; -; Genomic_DNA.
EnsemblBacteria; KZL05162; KZL05162; PsAD2_04517.
PATRIC; fig|989403.3.peg.4949; -.
Proteomes; UP000076577; Unassembled WGS sequence.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-UniRule.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.420; -; 1.
HAMAP; MF_00716; NosZ; 1.
InterPro; IPR002429; CcO_II-like_C.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR011045; N2O_reductase_N.
InterPro; IPR023644; NO_Rdtase.
InterPro; IPR006311; TAT_signal.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
SUPFAM; SSF49503; SSF49503; 1.
SUPFAM; SSF50974; SSF50974; 1.
TIGRFAMs; TIGR04244; nitrous_NosZ_RR; 1.
PROSITE; PS50857; COX2_CUA; 1.
PROSITE; PS51318; TAT; 1.
3: Inferred from homology;
Calcium {ECO:0000256|HAMAP-Rule:MF_00716};
Complete proteome {ECO:0000313|Proteomes:UP000076577};
Copper {ECO:0000256|HAMAP-Rule:MF_00716};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00716};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00716,
ECO:0000313|EMBL:KZL05162.1};
Periplasm {ECO:0000256|HAMAP-Rule:MF_00716};
Reference proteome {ECO:0000313|Proteomes:UP000076577};
Signal {ECO:0000256|HAMAP-Rule:MF_00716}.
DOMAIN 544 645 COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
REGION 547 645 COX2-like. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 140 140 Copper Z2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 141 141 Copper Z3. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 189 189 Copper Z2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 266 266 Calcium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00716}.
METAL 269 269 Calcium 2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 277 277 Calcium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00716}.
METAL 283 283 Calcium 2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 330 330 Calcium 2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 332 332 Copper Z1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 387 387 Copper Z1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 438 438 Copper Z3. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 459 459 Calcium 1; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00716}.
METAL 474 474 Calcium 1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 499 499 Copper Z4. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 588 588 Copper A1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 623 623 Copper A1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 623 623 Copper A2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 625 625 Copper A2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00716}.
METAL 627 627 Copper A1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 627 627 Copper A2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 631 631 Copper A2. {ECO:0000256|HAMAP-
Rule:MF_00716}.
METAL 634 634 Copper A1. {ECO:0000256|HAMAP-
Rule:MF_00716}.
SEQUENCE 645 AA; 71357 MW; 5FD033B9C01A9FC4 CRC64;
MTGKMNEVKR KGLSRRQMLG ASAAGAVGTG GLALLGGAAS LTATSALSPA MASGRGVELQ
PGELDPYYGF WSSGQCGELR ILGFPSMREL MRVPVFNRCS ATGWGQTNES LKVLTEGLTP
ETKDFLAKQG KKTYDNGDLH HPHMSYTDGT YDGRYVFMND KANTRVARVR VDVMKCDKIL
EIPNAHDIHG LRPQKYPRTG YVFANGEHEA PLINDGTILD EPDKYVNIFT AIDGDTMEVA
WQVMVSGNLD NCDCDYQGKY AYSTSYNSEM GMNLAEMTAG EMDHVVVFNL AEIEAAVKSG
DYQELNGIPV IDGRKGVNKK YTRYIPIPNS PHGINTVPDQ KHVVVNGKLS PTCSVLDVRK
FDAMFEEDVD PRSVVVAEPE LGLGPLHTAF DGKGFCYTTL FLDSQMVKWN LEKAIRKFNG
EDVDPIVSKV DVQYQPGHNH TTMGETTEAD GNWLISLNKF SKDRFLNVGP LKPENEQIID
ISSDDMKVVH DGPTFAEPHD CIMVRSDIVN PDNFWKRDDP MFADAVAQAK ADGVDPESDS
VVIRDGNKVR VYMTSMAPVF GLEKFTVKEG DEVTIIITNI DDIDDLTHGF TLGNYGLAME
LAPLATSSVT FTADRPGVHW YYCQWFCHAL HMEMRGRMFV EPKEA


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