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UniProtKB/Swiss-Prot entry Q9CPL4


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

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Entry information
Entry name NRFA_PASMU
Primary accession number Q9CPL4
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 55)
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: PM0023
From
Pasteurella multocida [TaxID: 747] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Pasteurella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Pm70;
DOI=10.1073/pnas.051634598; PubMed=11248100 [NCBI, ExPASy, EBI, Israel, Japan]
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
"Complete genomic sequence of Pasteurella multocida Pm70.";
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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
AE006035; AAK02107.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_244960.1; -.
3D structure databases
HSSP P32050; 1GU6. [HSSP ENTRY / PDB]
ModBase Q9CPL4.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from HAMAP).
GO:0042279; Molecular function: nitrite reductase (cytochrome, ammonia-forming) activity (inferred from electronic annotation from HAMAP).
GO:0006807; Biological process: nitrogen compound metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01182; -; 1.
PBIL [Tree]
InterPro IPR003321; Cyt_c552.
IPR017570; Cytc_552_NO2Rdtase_formate-dep.
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 Q9CPL4.
Genome annotation databases
GeneID 1243370; -.
GenomeReviews AE004439_GR; PM0023.
KEGG pmu:PM0023; -.
NMPDR fig|272843.1.peg.23; -.
Phylogenomic databases
HOGENOM Q9CPL4; -.
Genome annotation databases
CMR Q9CPL4; PM0023.
Other
ProtoNet Q9CPL4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    50  50     Potential. 
CHAIN   51   510  460     Cytochrome c-552. PRO_0000006580
METAL   124   124        Iron (heme 3 axial ligand) (By similarity). 
METAL   156   156        Iron (heme 1 axial ligand) (By similarity). 
METAL   194   194        Iron (heme 2 axial ligand) (By similarity). 
METAL   243   243        Iron (heme 3 axial ligand) (By similarity). 
METAL   245   245        Calcium (By similarity). 
METAL   246   246        Calcium; via carbonyl oxygen (By similarity). 
METAL   291   291        Calcium; via carbonyl oxygen (By similarity). 
METAL   293   293        Calcium (By similarity). 
METAL   305   305        Iron (heme 5 axial ligand) (By similarity). 
METAL   316   316        Iron (heme 4 axial ligand) (By similarity). 
METAL   331   331        Iron (heme 2 axial ligand) (By similarity). 
METAL   348   348        Iron (heme 5 axial ligand) (By similarity). 
METAL   423   423        Iron (heme 4 axial ligand) (By similarity). 
BINDING   152   152        Heme 1 (covalent) (By similarity). 
BINDING   155   155        Heme 1 (covalent) (By similarity). 
BINDING   190   190        Heme 2 (covalent) (By similarity). 
BINDING   193   193        Heme 2 (covalent) (By similarity). 
BINDING   239   239        Heme 3 (covalent) (By similarity). 
BINDING   242   242        Heme 3 (covalent) (By similarity). 
BINDING   246   246        Substrate (By similarity). 
BINDING   294   294        Substrate (By similarity). 
BINDING   312   312        Heme 4 (covalent) (By similarity). 
BINDING   315   315        Heme 4 (covalent) (By similarity). 
BINDING   344   344        Heme 5 (covalent) (By similarity). 
BINDING   347   347        Heme 5 (covalent) (By similarity). 
Sequence information
Length: 510 AA [This is the length of the unprocessed precursor] Molecular weight: 57260 Da [This is the MW of the unprocessed precursor] CRC64: 40A2695C513DBC43 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVFLFILYR QSDLKFKSMN GVIIVNTLKK RLFVATTMIW GLSVTLPVLA EYKPIEQPVE 

        70         80         90        100        110        120 
PANPSLKIES RNDLFKEKYP KQYQTWADTS KSTDLDSVNY EDPRVIVLWA GYAFAKDYKK 

       130        140        150        160        170        180 
PRGHFYAVTD VREILRTAAP MTPDAGPMPM ACWSCKSPDV PRLIAERGEA GYFGATWASG 

       190        200        210        220        230        240 
GSEVVNPIGC ADCHDTTSKD FAEGKPALRI ARPYVLRALE KIDHKFDTSD RTDQRAALCA 

       250        260        270        280        290        300 
NCHVEYYFAG DLKQVTFPWD NGITVDAMEK YYDDIGFVDW THAVSKAPML KAQHPDYETW 

       310        320        330        340        350        360 
MLGVHGKNGV TCIDCHMPKV QGADGKVYTD HQIGNPFNAF EHTCANCHDQ SKEKLQAMVK 

       370        380        390        400        410        420 
SRKTEIKDVM LRLEDQLVAA HFEAKAAWEA GATKEEMKEA LQDIRHAQWR WDYAAAGHGG 

       430        440        450        460        470        480 
HIHAPDVLLK VIGTGLDKSS DARTKLVRVL AKHGITDPVQ LPDISTAENA WKATGVDIEK 

       490        500        510 
ERKAKAEFLK TVVPQWDKEA REKGLLPAEK 

Q9CPL4 in FASTA format

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