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UniProtKB/Swiss-Prot entry Q9S1E5

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

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Entry information
Entry name NRFA_WOLSU
Primary accession number Q9S1E5
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on September 26, 2003 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 72)
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
OrderedLocusNames: WS0969
From
Wolinella succinogenes [TaxID: 844] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Wolinella.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-30, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=10672190 [NCBI, ExPASy, EBI, Israel, Japan]
Simon J., Gross R., Einsle O., Kroneck P.M.H., Kroeger A., Klimmek O.;
"A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes.";
Mol. Microbiol. 35:686-696(2000).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSMZ 1740;
DOI=10.1073/pnas.1932838100; PubMed=14500908 [NCBI, ExPASy, EBI, Israel, Japan]
Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C.;
"Complete genome sequence and analysis of Wolinella succinogenes.";
Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
[3]
 X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 37-507.
DOI=10.1074/jbc.M006188200; PubMed=10984487 [NCBI, ExPASy, EBI, Israel, Japan]
Einsle O., Stach P., Messerschmidt A., Simon J., Kroeger A., Huber R., Kroneck P.M.H.;
"Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs.";
J. Biol. Chem. 275:39608-39616(2000).
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
AJ245540; CAB53160.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX571659; CAE10072.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_907172.1; -.
3D structure databases
PDB
1FS7; X-ray; 1.60 A; A=23-507.[ExPASy / RCSB / EBI]
1FS8; X-ray; 1.60 A; A=23-507.[ExPASy / RCSB / EBI]
1FS9; X-ray; 2.00 A; A=1-507.[ExPASy / RCSB / EBI]
2E80; X-ray; 1.60 A; A=23-507.[ExPASy / RCSB / EBI]
2E81; X-ray; 2.00 A; A=23-507.[ExPASy / RCSB / EBI]
3BNF; X-ray; 1.70 A; A=23-507.[ExPASy / RCSB / EBI]
3BNG; X-ray; 1.50 A; A=23-507.[ExPASy / RCSB / EBI]
3BNH; X-ray; 1.75 A; A=23-507.[ExPASy / RCSB / EBI]
3BNJ; X-ray; 1.30 A; A=23-507.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FS7; -.
1FS8; -.
1FS9; -.
2E80; -.
2E81; -.
3BNF; -.
3BNG; -.
3BNH; -.
3BNJ; -.
ModBase Q9S1E5.
Enzyme and pathway databases
BioCyc WSUC273121:WS0969-MON; -.
Ontologies
GO
GO:0030288; Cellular component: outer membrane-bounded periplasmic space (inferred from direct assay from UniProtKB).
GO:0006807; Biological process: nitrogen compound metabolic process (inferred from direct assay from UniProtKB).
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).
BLOCKS Q9S1E5.
Genome annotation databases
GeneID 2555567; -.
GenomeReviews BX571656_GR; WS0969.
KEGG wsu:WS0969; -.
NMPDR fig|273121.1.peg.899; -.
Phylogenomic databases
HOGENOM Q9S1E5; -.
Genome annotation databases
CMR Q9S1E5; WS0969.
Other
ProtoNet Q9S1E5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   507  485     Cytochrome c-552. PRO_0000006584
METAL   102   102        Iron (heme 3 axial ligand). 
METAL   134   134        Iron (heme 1 axial ligand). 
METAL   172   172        Iron (heme 2 axial ligand). 
METAL   215   215        Iron (heme 3 axial ligand). 
METAL   217   217        Calcium. 
METAL   218   218        Calcium (via carbonyl oxygen). 
METAL   274   274        Calcium (via carbonyl oxygen). 
METAL   276   276        Calcium. 
METAL   288   288        Iron (heme 5 axial ligand). 
METAL   299   299        Iron (heme 4 axial ligand). 
METAL   313   313        Iron (heme 2 axial ligand). 
METAL   330   330        Iron (heme 5 axial ligand). 
METAL   405   405        Iron (heme 4 axial ligand). 
BINDING   130   130        Heme 1 (covalent). 
BINDING   133   133        Heme 1 (covalent). 
BINDING   168   168        Heme 2 (covalent). 
BINDING   171   171        Heme 2 (covalent). 
BINDING   211   211        Heme 3 (covalent). 
BINDING   214   214        Heme 3 (covalent). 
BINDING   218   218        Substrate. 
BINDING   277   277        Substrate. 
BINDING   295   295        Heme 4 (covalent). 
BINDING   298   298        Heme 4 (covalent). 
BINDING   326   326        Heme 5 (covalent). 
BINDING   329   329        Heme 5 (covalent). 
CONFLICT   45    45        E -> K (in Ref. 1; CAB53160). 
TURN   39    42  4      
TURN   45    48  4      
HELIX   50    53  4      
TURN   54    56  3      
HELIX   58    65  8      
HELIX   66    69  4      
HELIX   76    79  4      
HELIX   82    86  5      
TURN   87    89  3      
HELIX   91    93  3      
HELIX   102   104  3      
HELIX   105   111  7      
HELIX   113   115  3      
STRAND   124   127  4      
HELIX   128   131  4      
TURN   132   134  3      
HELIX   137   145  9      
HELIX   147   150  4      
STRAND   152   154  3      
HELIX   155   158  4      
TURN   159   161  3      
HELIX   168   171  4      
TURN   174   176  3      
HELIX   185   192  8      
TURN   198   200  3      
HELIX   203   212  10      
STRAND   219   226  8      
STRAND   232   239  8      
HELIX   248   257  10      
STRAND   262   264  3      
TURN   266   268  3      
HELIX   279   285  7      
HELIX   287   290  4      
HELIX   295   299  5      
STRAND   302   305  4      
STRAND   308   311  4      
HELIX   318   321  4      
HELIX   322   325  4      
TURN   326   329  4      
HELIX   334   372  39      
HELIX   376   397  22      
HELIX   402   405  4      
HELIX   407   434  28      
HELIX   448   454  7      
HELIX   459   471  13      
HELIX   473   483  11      
HELIX   489   492  4      
TURN   493   496  4      
Sequence information
Length: 507 AA [This is the length of the unprocessed precursor] Molecular weight: 57511 Da [This is the MW of the unprocessed precursor] CRC64: D5CE7E841E3E7AB3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTKFKLLLAG SLVAIVSMGL LASNINEREK ERVALNKTAH SQGIEGKAMS EEWARYYPRQ 

        70         80         90        100        110        120 
FDSWKKTKES DNITDMLKEK PALVVAWAGY PFSKDYNAPR GHYYALQDNI NTLRTGAPVD 

       130        140        150        160        170        180 
GKTGPLPSAC WTCKSPDVPR IIEQDGELEY FTGKWAKYGD EIVNTIGCYN CHDDKSAELK 

       190        200        210        220        230        240 
SKVPYLDRGL SAAGFKTFAE STHQEKRSLV CAQCHVEYYF KKTEWKDDKG VDKTAMVVTL 

       250        260        270        280        290        300 
PWSKGISTEQ MEAYYDEINF ADWTHGISKT PMLKAQHPDW ELYKTGIHGQ KGVSCADCHM 

       310        320        330        340        350        360 
PYTQEGAVKY SDHKVGNPLD NMDKSCMNCH RESEQKLKDI VKQKFERKEF LQDIAFDNIG 

       370        380        390        400        410        420 
KAHLETGKAM ELGATDAELK EIRTHIRHAQ WRADMAIAGH GSFFHAPEEV LRLLASGNEE 

       430        440        450        460        470        480 
AQKARIKLVK VLAKYGAIDY VAPDFETKEK AQKLAKVDME AFIAEKLKFK QTLEQEWKKQ 

       490        500 
AIAKGRLNPE SLKGVDEKSS YYDKTKK
Q9S1E5 in FASTA format

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