MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Nitrous-oxide reductase; EC=1.7.2.4; AltName: Full=N(2)OR; AltName: Full=N2O reductase; Flags: Precursor; |
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| MyHits synonyms | NOSZ_BRADU , Q89XJ6 , O31382 , 1B6C547D90501C5B |
 Legends: 1, Copper Z2. {ECO:0000250}; 2, Copper Z3. {ECO:0000250}; 3, Calcium 2; via carbonyl oxygen. {ECO:0000250}; 4, Calcium 2. {ECO:0000250}; 5, Copper Z1. {ECO:0000250}; 6, Calcium 1; via carbonyl oxygen. {ECO:0000250}; 7, Calcium 1. {ECO:0000250}; 8, Copper Z4. {ECO:0000250}; 9, Copper A1. {ECO:0000250}; 10, Copper A2. {ECO:0000250}; 11, Copper A2; via carbonyl oxygen. {ECO:0000250}; 12, CONFLICT D -> N (in Ref. 1; CAA05518). {ECO:0000305}; 13, SIGNAL Tat-type signal. {ECO:0000255}; 14, ipfam:Cupredoxin_1 [T]; 15, iprf:TAT [T].
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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 15-MAR-2017, entry version 102.
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 / IAM 13628 / NBRC
OS 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / 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 / 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.,
RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA 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
CC respiratory system which is activated under anaerobic conditions
CC in the presence of nitrate or nitrous oxide. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: Nitrogen + H(2)O + 2 ferricytochrome c =
CC nitrous oxide + 2 ferrocytochrome c + 2 H(+).
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
CC copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z)
CC is thought to be the site of nitrous oxide reduction.
CC {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
CC the 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 ProteinModelPortal; Q89XJ6; -.
DR SMR; Q89XJ6; -.
DR STRING; 224911.blr0315; -.
DR EnsemblBacteria; BAC45580; BAC45580; BAC45580.
DR GeneID; 1052167; -.
DR KEGG; bja:blr0315; -.
DR PATRIC; 21184065; VBIBraJap65052_0312.
DR eggNOG; ENOG4105EQJ; Bacteria.
DR eggNOG; COG4263; LUCA.
DR HOGENOM; HOG000028241; -.
DR InParanoid; Q89XJ6; -.
DR KO; K00376; -.
DR OMA; HQEMQGY; -.
DR OrthoDB; POG091H0M5N; -.
DR PhylomeDB; Q89XJ6; -.
DR BRENDA; 1.7.2.4; 929.
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:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-EC.
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; IPR006311; TAT_signal.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR Pfam; PF13473; Cupredoxin_1; 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; Complete proteome; Copper; Metal-binding; Oxidoreductase;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1 46 Tat-type signal. {ECO:0000255}.
FT CHAIN 47 650 Nitrous-oxide reductase.
FT /FTId=PRO_0000019824.
FT REGION 552 650 COX2-like.
FT METAL 147 147 Copper Z2. {ECO:0000250}.
FT METAL 148 148 Copper Z3. {ECO:0000250}.
FT METAL 196 196 Copper Z2. {ECO:0000250}.
FT METAL 273 273 Calcium 2; via carbonyl oxygen.
FT {ECO:0000250}.
FT METAL 276 276 Calcium 2. {ECO:0000250}.
FT METAL 284 284 Calcium 2; via carbonyl oxygen.
FT {ECO:0000250}.
FT METAL 290 290 Calcium 2. {ECO:0000250}.
FT METAL 335 335 Calcium 2. {ECO:0000250}.
FT METAL 337 337 Copper Z1. {ECO:0000250}.
FT METAL 392 392 Copper Z1. {ECO:0000250}.
FT METAL 443 443 Copper Z3. {ECO:0000250}.
FT METAL 464 464 Calcium 1; via carbonyl oxygen.
FT {ECO:0000250}.
FT METAL 479 479 Calcium 1. {ECO:0000250}.
FT METAL 504 504 Copper Z4. {ECO:0000250}.
FT METAL 593 593 Copper A1. {ECO:0000250}.
FT METAL 628 628 Copper A1. {ECO:0000250}.
FT METAL 628 628 Copper A2. {ECO:0000250}.
FT METAL 630 630 Copper A2; via carbonyl oxygen.
FT {ECO:0000250}.
FT METAL 632 632 Copper A1. {ECO:0000250}.
FT METAL 632 632 Copper A2. {ECO:0000250}.
FT METAL 636 636 Copper A2. {ECO:0000250}.
FT METAL 639 639 Copper A1. {ECO:0000250}.
FT CONFLICT 367 367 D -> N (in Ref. 1; CAA05518).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 556 645 ipfam:Cupredoxin_1 [T]
FT MYHIT 549 650 iprf:COX2_CUA [T]
FT MYHIT 1 46 iprf:TAT [T]
FT MYHIT 2 647 ihamap:NosZ [T]
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
//
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