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UniProtKB/Swiss-Prot entry P72181


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

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Entry information
Entry name NIRS_PARPN
Primary accession number P72181
Secondary accession number Q9FCQ0
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 8, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 70)
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
From
Paracoccus pantotrophus (Thiosphaera pantotropha) [TaxID: 82367] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Paracoccus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LMD 92.63;
PubMed=10708389 [NCBI, ExPASy, EBI, Israel, Japan]
Saunders N.F.W., Ferguson S.J., Baker S.C.;
"Transcriptional analysis of the nirS gene, encoding cytochrome cd1 nitrite reductase, of Paracoccus pantotrophus LMD 92.63.";
Microbiology 146:509-516(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/bbrc.2001.4425; PubMed=11237728 [NCBI, ExPASy, EBI, Israel, Japan]
Gordon E.H.J., Steensma E., Ferguson S.J.;
"The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli.";
Biochem. Biophys. Res. Commun. 281:788-794(2001).
[3]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
DOI=10.1016/0092-8674(95)90390-9; PubMed=7736589 [NCBI, ExPASy, EBI, Israel, Japan]
Fueloep V., Moir J.W.B., Ferguson S.J., Hajdu J.;
"The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1.";
Cell 81:369-377(1995).
[4]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
DOI=10.1006/jmbi.1997.1070; PubMed=9199411 [NCBI, ExPASy, EBI, Israel, Japan]
Baker S.C., Saunders N.F.W., Willis A.C., Ferguson S.J., Fueloep V., Hajdu J.;
"Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.";
J. Mol. Biol. 269:440-455(1997).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/38775; PubMed=9311786 [NCBI, ExPASy, EBI, Israel, Japan]
Williams P.A., Fueloep V., Garman E.F., Saunders N.F.W., Ferguson S.J., Hajdu J.;
"Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.";
Nature 389:406-412(1997).
[6]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1021/bi000179q; PubMed=10998233 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoegren T., Svensson-Ek M., Hajdu J., Brzezinski P.;
"Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study.";
Biochemistry 39:10967-10974(2000).
[7]
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).
DOI=10.1074/jbc.M001377200; PubMed=10827177 [NCBI, ExPASy, EBI, Israel, Japan]
Jafferji A., Allen J.W.A., Ferguson S.J., Fueloep V.;
"X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.";
J. Biol. Chem. 275:25089-25094(2000).
[8]
X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS).
DOI=10.1074/jbc.M011312200; PubMed=11278884 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoegren T., Hajdu J.;
"Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.";
J. Biol. Chem. 276:13072-13076(2001).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1074/jbc.M103657200; PubMed=11373294 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoegren T., Hajdu J.;
"The structure of an alternative form of Paracoccus pantotrophus cytochrome cd1 nitrite reductase.";
J. Biol. Chem. 276:29450-29455(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
U75413; AAB17878.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ401462; CAC03621.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1AOF; X-ray; 2.00 A; A/B=30-596.[ExPASy / RCSB / EBI]
1AOM; X-ray; 1.80 A; A/B=30-596.[ExPASy / RCSB / EBI]
1AOQ; X-ray; 1.80 A; A/B=30-596.[ExPASy / RCSB / EBI]
1DY7; X-ray; 1.60 A; A/B=30-596.[ExPASy / RCSB / EBI]
1E2R; X-ray; 1.59 A; A/B=30-596.[ExPASy / RCSB / EBI]
1GQ1; X-ray; 1.40 A; A/B=30-596.[ExPASy / RCSB / EBI]
1H9X; X-ray; 2.10 A; A/B=30-596.[ExPASy / RCSB / EBI]
1H9Y; X-ray; 2.40 A; A/B=30-596.[ExPASy / RCSB / EBI]
1HCM; X-ray; 2.50 A; A/B=30-596.[ExPASy / RCSB / EBI]
1HJ3; X-ray; 1.60 A; A/B=30-596.[ExPASy / RCSB / EBI]
1HJ4; X-ray; 1.60 A; A/B=30-596.[ExPASy / RCSB / EBI]
1HJ5; X-ray; 1.46 A; A/B=30-596.[ExPASy / RCSB / EBI]
1QKS; X-ray; 1.28 A; A/B=30-596.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AOF; -.
1AOM; -.
1AOQ; -.
1DY7; -.
1E2R; -.
1GQ1; -.
1H9X; -.
1H9Y; -.
1HCM; -.
1HJ3; -.
1HJ4; -.
1HJ5; -.
1QKS; -.
ModBase P72181.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0050418; Molecular function: hydroxylamine reductase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050421; Molecular function: nitrite reductase (NO-forming) activity (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0046209; Biological process: nitric oxide metabolic process (inferred from electronic annotation from InterPro).
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).
ProtoNet P72181.
Other
LinkHub P72181; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 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    29  29      
CHAIN   30   596  567     Nitrite reductase. PRO_0000006575
DOMAIN   77   162  86     Cytochrome c. 
REGION   30    76  47     N-terminal tail. 
REGION   163   596  434     D1-heme domain. 
METAL   46    46        Iron (heme axial ligand). 
METAL   98    98        Iron (heme axial ligand). 
METAL   229   229        Iron (heme D1 proximal ligand). 
BINDING   94    94        Heme (covalent). 
BINDING   97    97        Heme (covalent). 
CONFLICT   28    28        S -> A (in Ref. 1; AAB17878). 
CONFLICT   76    76        S -> T (in Ref. 1; AAB17878). 
CONFLICT   130   130        G -> A (in Ref. 1; AAB17878). 
CONFLICT   214   214        A -> T (in Ref. 1; AAB17878). 
HELIX   39    41  3      
HELIX   42    45  4      
HELIX   61    63  3      
HELIX   80    93  14      
HELIX   95    98  4      
STRAND   105   107  3      
HELIX   112   118  7      
HELIX   120   127  8      
TURN   136   138  3      
HELIX   146   156  11      
HELIX   168   174  7      
STRAND   176   179  4      
HELIX   181   183  3      
HELIX   194   196  3      
STRAND   197   202  6      
HELIX   203   205  3      
STRAND   207   212  6      
TURN   213   215  3      
STRAND   218   223  6      
STRAND   228   233  6      
STRAND   239   244  6      
STRAND   247   253  7      
STRAND   256   258  3      
STRAND   261   266  6      
STRAND   269   276  8      
TURN   283   285  3      
STRAND   286   293  8      
STRAND   296   301  6      
TURN   302   304  3      
STRAND   307   312  6      
TURN   318   320  3      
STRAND   323   325  3      
STRAND   329   334  6      
STRAND   336   345  10      
TURN   346   349  4      
STRAND   350   355  6      
STRAND   359   368  10      
STRAND   373   378  6      
STRAND   384   389  6      
HELIX   390   392  3      
STRAND   394   399  6      
TURN   400   403  4      
STRAND   404   410  7      
STRAND   412   416  5      
STRAND   422   426  5      
TURN   427   429  3      
STRAND   430   447  18      
TURN   450   452  3      
TURN   454   456  3      
STRAND   459   465  7      
STRAND   481   485  5      
HELIX   493   496  4      
STRAND   499   503  5      
HELIX   504   506  3      
STRAND   510   512  3      
STRAND   516   519  4      
HELIX   521   525  5      
STRAND   533   539  7      
STRAND   543   551  9      
STRAND   559   564  6      
TURN   565   568  4      
STRAND   569   574  6      
STRAND   581   587  7      
HELIX   588   592  5      
Sequence information
Length: 596 AA [This is the length of the unprocessed precursor] Molecular weight: 65383 Da [This is the MW of the unprocessed precursor] CRC64: ABAD0C871E8FB7F1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRQRTPFARP GLLASAALAL VLGPLAASAQ EQVAPPKDPA AALEDHKTRT DNRYEPSLDN 

        70         80         90        100        110        120 
LAQQDVAAPG APEGVSALSD AQYNEANKIY FERCAGCHGV LRKGATGKAL TPDLTRDLGF 

       130        140        150        160        170        180 
DYLQSFITYG SPAGMPNWGT SGELSAEQVD LMANYLLLDP AAPPEFGMKE MRESWKVHVA 

       190        200        210        220        230        240 
PEDRPTQQEN DWDLENLFSV TLRDAGQIAL IDGATYEIKS VLDTGYAVHI SRLSASGRYL 

       250        260        270        280        290        300 
FVIGRDGKVN MIDLWMKEPT TVAEIKIGSE ARSIETSKME GWEDKYAIAG AYWPPQYVIM 

       310        320        330        340        350        360 
DGETLEPKKI QSTRGMTYDE QEYHPEPRVA AILASHYRPE FIVNVKETGK ILLVDYTDLD 

       370        380        390        400        410        420 
NLKTTEISAE RFLHDGGLDG SHRYFITAAN ARNKLVVIDT KEGKLVAIED TGGQTPHPGR 

       430        440        450        460        470        480 
GANFVHPTFG PVWATSHMGD DSVALIGTDP EGHPDNAWKI LDSFPALGGG SLFIKTHPNS 

       490        500        510        520        530        540 
QYLYVDATLN PEAEISGSVA VFDIKAMTGD GSDPEFKTLP IAEWAGITEG QPRVVQGEFN 

       550        560        570        580        590 
KDGTEVWFSV WNGKDQESAL VVVDDKTLEL KHVIKDERLV TPTGKFNVYN TMTDTY 

P72181 in FASTA format

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View entry in raw text format (no links)
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