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UniProtKB/Swiss-Prot entry P24474


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NIRS_PSEAE
Primary accession number P24474
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on March 1, 1992 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 83)
Name and origin of the protein
Protein name Nitrite reductase [Precursor]
Synonyms EC 1.7.2.1
Cytochrome cd1
Cytochrome oxidase
Hydroxylamine reductase
EC 1.7.99.1
Gene name
Name: nirS
OrderedLocusNames: PA0519
From
Pseudomonas aeruginosa [TaxID: 287] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-70.
STRAIN=NTCC 6750;
DOI=10.1016/0014-5793(89)81004-X; PubMed=2506077 [NCBI, ExPASy, EBI, Israel, Japan]
Silvestrini M.C., Galeotti C.L., Gervais M., Schinina E., Barra D., Bossa F., Brunori M.;
"Nitrite reductase from Pseudomonas aeruginosa: sequence of the gene and the protein.";
FEBS Lett. 254:33-38(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-568.
DOI=10.1016/0014-5793(90)80669-A; PubMed=2155133 [NCBI, ExPASy, EBI, Israel, Japan]
Arai H., Sanbongi Y., Igarashi Y., Kodama T.;
"Cloning and sequencing of the gene encoding cytochrome c-551 from Pseudomonas aeruginosa.";
FEBS Lett. 261:196-198(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-568.
STRAIN=ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NCIMB 8295;
DOI=10.1016/0014-5793(90)80015-B; PubMed=2152881 [NCBI, ExPASy, EBI, Israel, Japan]
Nordling M., Young S., Karlsson B.G., Lundberg L.G.;
"The structural gene for cytochrome c551 from Pseudomonas aeruginosa. The nucleotide sequence shows a location downstream of the nitrite reductase gene.";
FEBS Lett. 259:230-232(1990).
[5]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
STRAIN=NTCC 6750;
DOI=10.1016/S0969-2126(97)00267-0; PubMed=9331415 [NCBI, ExPASy, EBI, Israel, Japan]
Nurizzo D., Silvestrini M.-C., Mathieu M., Cutruzzola F., Bourgeois D., Fueloep V., Hajdu J., Brunori M., Tegoni M., Cambillau C.;
"N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa.";
Structure 5:1157-1171(1997).
[6]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
STRAIN=NTCC 6750;
DOI=10.1021/bi981348y; PubMed=9760233 [NCBI, ExPASy, EBI, Israel, Japan]
Nurizzo D., Cutruzzola F., Arese M., Bourgeois D., Brunori M., Cambillau C., Tegoni M.;
"Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa.";
Biochemistry 37:13987-13996(1998).
[7]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
STRAIN=NTCC 6750;
DOI=10.1074/jbc.274.21.14997; PubMed=10329702 [NCBI, ExPASy, EBI, Israel, Japan]
Nurizzo D., Cutruzzola F., Arese M., Bourgeois D., Brunori M., Cambillau C., Tegoni M.;
"Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?";
J. Biol. Chem. 274:14997-15004(1999).
[8]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF H394A AND H352A MUTANTS.
DOI=10.1073/pnas.041365298; PubMed=11226222 [NCBI, ExPASy, EBI, Israel, Japan]
Cutruzzola F., Brown K., Wilson E.K., Bellelli A., Arese M., Tegoni M., Cambillau C., Brunori B.;
"The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties.";
Proc. Natl. Acad. Sci. U.S.A. 98:2232-2237(2001).
[9]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF H394A AND H352A MUTANTS.
DOI=10.1006/jmbi.2001.4986; PubMed=11563915 [NCBI, ExPASy, EBI, Israel, Japan]
Brown K., Roig-Zamboni V., Cutruzzola F., Arese M., Sun W., Brunori M., Cambillau C., Tegoni M.;
"Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa.";
J. Mol. Biol. 312:541-554(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X16452; CAA34471.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG03908.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51631; CAA35957.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51319; CAA35702.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32975; OSPSA.
RefSeq NP_249210.1; -.
3D structure databases
PDB
1BL9; X-ray; 2.90 A; A/B=26-568.[ExPASy / RCSB / EBI]
1GJQ; X-ray; 2.70 A; A/B=26-568.[ExPASy / RCSB / EBI]
1HZU; X-ray; 2.70 A; A=26-568.[ExPASy / RCSB / EBI]
1HZV; X-ray; 2.83 A; A=26-568.[ExPASy / RCSB / EBI]
1N15; X-ray; 2.90 A; A/B=26-568.[ExPASy / RCSB / EBI]
1N50; X-ray; 2.90 A; A/B=26-568.[ExPASy / RCSB / EBI]
1N90; X-ray; 2.90 A; A/B=26-568.[ExPASy / RCSB / EBI]
1NIR; X-ray; 2.15 A; A/B=26-568.[ExPASy / RCSB / EBI]
1NNO; X-ray; 2.65 A; A/B=26-568.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BL9; -.
1GJQ; -.
1HZU; -.
1HZV; -.
1N15; -.
1N50; -.
1N90; -.
1NIR; -.
1NNO; -.
ModBase P24474.
Enzyme and pathway databases
BioCyc PAER208964:PA0519-MON; -.
Organism-specific databases
PseudoCAP PA0519; -.
Ontologies
GO
GO:0050418; Molecular function: hydroxylamine reductase activity (inferred from electronic annotation from EC).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR009056; Cyt_c_monohaem.
IPR003088; Cyt_CI.
IPR003143; Cyt_d1_haem.
Graphical view of domain structure.
Gene3D G3DSA:2.140.10.20; Cyt_d1_haem; 1.
G3DSA:1.10.760.10; Cytochrome_c_R; 1.
Pfam PF00034; Cytochrom_C; 1.
PF02239; Cytochrom_D1; 1.
Pfam graphical view of domain structure.
PROSITE PS51007; CYTC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P24474.
ProtoNet P24474.
Genome annotation databases
GeneID 882217; -.
GenomeReviews AE004091_GR; PA0519.
KEGG pae:PA0519; -.
NMPDR fig|208964.1.peg.520; -.
Phylogenomic databases
HOGENOM P24474; -.
Other
LinkHub P24474; -.
Genome annotation databases
CMR P24474; PA0519.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25      
CHAIN   26   568  543     Nitrite reductase. PRO_0000006576
DOMAIN   55   140  86     Cytochrome c. 
REGION   26    54  29     N-terminal tail. 
REGION   141   568  428     D1-heme domain. 
METAL   76    76        Iron (heme axial ligand). 
METAL   113   113        Iron (heme axial ligand). 
METAL   207   207        Iron (heme D1 proximal ligand). 
BINDING   72    72        Heme (covalent). 
BINDING   75    75        Heme (covalent). 
HELIX   32    35  4      
HELIX   44    46  3      
HELIX   58    71  14      
HELIX   73    76  4      
TURN   77    80  4      
STRAND   83    86  4      
HELIX   90    96  7      
HELIX   98   107  10      
STRAND   110   112  3      
TURN   117   120  4      
HELIX   124   133  10      
HELIX   146   152  7      
STRAND   154   157  4      
HELIX   159   161  3      
HELIX   172   174  3      
STRAND   175   180  6      
HELIX   181   183  3      
STRAND   185   190  6      
TURN   191   193  3      
STRAND   196   201  6      
STRAND   206   211  6      
STRAND   217   222  6      
STRAND   225   231  7      
STRAND   234   236  3      
STRAND   238   244  7      
STRAND   247   254  8      
TURN   261   263  3      
STRAND   264   279  16      
TURN   280   282  3      
STRAND   285   290  6      
STRAND   296   298  3      
STRAND   301   303  3      
STRAND   307   312  6      
STRAND   314   323  10      
TURN   324   327  4      
STRAND   328   333  6      
STRAND   337   339  3      
STRAND   341   346  6      
STRAND   354   356  3      
STRAND   362   367  6      
HELIX   368   370  3      
STRAND   372   377  6      
TURN   378   381  4      
STRAND   382   388  7      
STRAND   390   393  4      
STRAND   399   403  5      
TURN   404   406  3      
STRAND   407   424  18      
TURN   427   429  3      
TURN   431   433  3      
STRAND   436   442  7      
STRAND   459   462  4      
HELIX   470   473  4      
STRAND   476   480  5      
STRAND   489   491  3      
HELIX   493   497  5      
STRAND   505   511  7      
STRAND   513   523  11      
STRAND   531   536  6      
TURN   537   540  4      
STRAND   541   546  6      
STRAND   553   559  7      
HELIX   560   564  5      
Sequence information
Length: 568 AA [This is the length of the unprocessed precursor] Molecular weight: 62653 Da [This is the MW of the unprocessed precursor] CRC64: 20FAE9FFE9127D62 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPFGKPLVGT LLASLTLLGL ATAHAKDDMK AAEQYQGAAS AVDPAHVVRT NGAPDMSESE 

        70         80         90        100        110        120 
FNEAKQIYFQ RCAGCHGVLR KGATGKPLTP DITQQRGQQY LEALITYGTP LGMPNWGSSG 

       130        140        150        160        170        180 
ELSKEQITLM AKYIQHTPPQ PPEWGMPEMR ESWKVLVKPE DRPKKQLNDL DLPNLFSVTL 

       190        200        210        220        230        240 
RDAGQIALVD GDSKKIVKVI DTGYAVHISR MSASGRYLLV IGRDARIDMI DLWAKEPTKV 

       250        260        270        280        290        300 
AEIKIGIEAR SVESSKFKGY EDRYTIAGAY WPPQFAIMDG ETLEPKQIVS TRGMTVDTQT 

       310        320        330        340        350        360 
YHPEPRVAAI IASHEHPEFI VNVKETGKVL LVNYKDIDNL TVTSIGAAPF LHDGGWDSSH 

       370        380        390        400        410        420 
RYFMTAANNS NKVAVIDSKD RRLSALVDVG KTPHPGRGAN FVHPKYGPVW STSHLGDGSI 

       430        440        450        460        470        480 
SLIGTDPKNH PQYAWKKVAE LQGQGGGSLF IKTHPKSSHL YVDTTFNPDA RISQSVAVFD 

       490        500        510        520        530        540 
LKNLDAKYQV LPIAEWADLG EGAKRVVQPE YNKRGDEVWF SVWNGKNDSS ALVVVDDKTL 

       550        560 
KLKAVVKDPR LITPTGKFNV YNTQHDVY 

P24474 in FASTA format

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