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UniProtKB/Swiss-Prot entry Q9Z4P4

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

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Entry information
Entry name NRFA_SULDE
Primary accession number Q9Z4P4
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 68)
Name and origin of the protein
Protein name Cytochrome c-552 [Precursor]
Synonyms EC 1.7.2.2
Ammonia-forming cytochrome c nitrite reductase
Cytochrome c nitrite reductase
Gene name
Name: nrfA
From
Sulfurospirillum deleyianum [TaxID: 65553] 
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Sulfurospirillum.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1038/22802; PubMed=10440380 [NCBI, ExPASy, EBI, Israel, Japan]
Einsle O., Messerschmidt A., Stach P., Bourenkov G.P., Bartunik H.D., Huber R., Kroneck P.M.H.;
"Structure of cytochrome c nitrite reductase.";
Nature 400:476-480(1999).
[2]
 CATALYTIC ACTIVITY, SUBUNIT, AND HEME-BINDING.
DOI=10.1006/bbrc.1994.2751; PubMed=7999130 [NCBI, ExPASy, EBI, Israel, Japan]
Schumacher W., Hole U., Kroneck P.M.H.;
"Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties.";
Biochem. Biophys. Res. Commun. 205:911-916(1994).
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
AJ133037; CAB37320.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1QDB; X-ray; 1.90 A; A/B/C=42-514.[ExPASy / RCSB / EBI]
PDBsum 1QDB; -.
ModBase Q9Z4P4.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from HAMAP).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042279; Molecular function: nitrite reductase (cytochrome, ammonia-forming) activity (inferred from electronic annotation from HAMAP).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006807; Biological process: nitrogen compound metabolic process (inferred from electronic annotation from HAMAP).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01182; -; 1.
PBIL [Tree]
InterPro IPR003321; Cyt_c552.
IPR011031; Multihaem_cyt.
Graphical view of domain structure.
Pfam PF02335; Cytochrom_C552; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000243; Cyt_c552; 1.
PROSITE PS51008; MULTIHEME_CYTC; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Z4P4.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    21  21      
CHAIN   22   514  493     Cytochrome c-552. PRO_0000006583
METAL   101   101        Iron (heme 3 axial ligand). 
METAL   133   133        Iron (heme 1 axial ligand). 
METAL   171   171        Iron (heme 2 axial ligand). 
METAL   214   214        Iron (heme 3 axial ligand). 
METAL   216   216        Calcium. 
METAL   217   217        Calcium; via carbonyl oxygen. 
METAL   280   280        Calcium; via carbonyl oxygen. 
METAL   281   281        Calcium. 
METAL   293   293        Iron (heme 5 axial ligand). 
METAL   304   304        Iron (heme 4 axial ligand). 
METAL   318   318        Iron (heme 2 axial ligand). 
METAL   336   336        Iron (heme 5 axial ligand). 
METAL   411   411        Iron (heme 4 axial ligand). 
BINDING   129   129        Heme 1 (covalent). 
BINDING   132   132        Heme 1 (covalent). 
BINDING   167   167        Heme 2 (covalent). 
BINDING   170   170        Heme 2 (covalent). 
BINDING   210   210        Heme 3 (covalent). 
BINDING   213   213        Heme 3 (covalent). 
BINDING   217   217        Substrate. 
BINDING   282   282        Substrate. 
BINDING   300   300        Heme 4 (covalent). 
BINDING   303   303        Heme 4 (covalent). 
BINDING   332   332        Heme 5 (covalent). 
BINDING   335   335        Heme 5 (covalent). 
TURN   44    47  4      
HELIX   49    54  6      
HELIX   57    64  8      
HELIX   65    68  4      
HELIX   75    78  4      
HELIX   81    85  5      
TURN   86    88  3      
HELIX   90    92  3      
HELIX   101   103  3      
HELIX   104   110  7      
HELIX   112   114  3      
STRAND   123   126  4      
HELIX   127   130  4      
TURN   131   133  3      
HELIX   136   144  9      
HELIX   146   149  4      
STRAND   151   153  3      
HELIX   154   157  4      
TURN   158   160  3      
HELIX   167   170  4      
TURN   173   175  3      
HELIX   184   191  8      
HELIX   197   199  3      
HELIX   202   211  10      
STRAND   218   225  8      
STRAND   231   238  8      
STRAND   245   247  3      
HELIX   253   262  10      
STRAND   267   269  3      
TURN   271   273  3      
HELIX   284   290  7      
HELIX   292   295  4      
HELIX   300   304  5      
STRAND   307   310  4      
STRAND   313   316  4      
HELIX   324   327  4      
HELIX   328   331  4      
TURN   332   335  4      
HELIX   340   377  38      
TURN   382   385  4      
HELIX   386   404  19      
HELIX   408   411  4      
HELIX   413   440  28      
HELIX   454   461  8      
HELIX   465   477  13      
HELIX   479   489  11      
HELIX   495   497  3      
HELIX   499   501  3      
Sequence information
Length: 514 AA [This is the length of the unprocessed precursor] Molecular weight: 57611 Da [This is the MW of the unprocessed precursor] CRC64: E63C119D4FA98562 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKFKLLLAGS LVAVGAMALL ASNINEKEKQ RVELAKAPSE AGIAGKEKSE EWAKYYPRQF 

        70         80         90        100        110        120 
DSWKKTKEYD SFTDMLAKDP ALVIAWSGYA FSKDYNSPRG HYYALQDNVN SLRTGAPVDA 

       130        140        150        160        170        180 
KTGPLPTACW TCKSPDVPRL IEEDGELEYF TGKWAKYGSQ IVNVIGCANC HDDKTAELKV 

       190        200        210        220        230        240 
RVPHLNRGLQ AAGLKTFEES THQDKRTLVC AQCHVEYYFK KTEWKDAKGA DKTAMVVTLP 

       250        260        270        280        290        300 
WANGVGKDGN AGVEGMIKYY DEINFSDWTH NISKTPMLKA QHPGFEFWKS GIHGQKGVSC 

       310        320        330        340        350        360 
ADCHMPYTQE GSVKYSDHQV KENPLDSMDQ SCMNCHRESE SKLRGIVHQK YERKEFLNKV 

       370        380        390        400        410        420 
AFDNIGKAHL ETGKAIEAGA SDEELKEVRK LIRHGQFKAD MAIAAHGNYF HAPEETLRLL 

       430        440        450        460        470        480 
AAGSDDAQKA RLLLVKILAK HGVMDYIAPD FDTKDKAQKL AKVDIAALAA EKMKFKQTLE 

       490        500        510 
QEWKKEAKAK GRANPELYKD VDTINDGKSS WNKK
Q9Z4P4 in FASTA format

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