ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q7VNX8

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name NRFA_HAEDU
Primary accession number Q7VNX8
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on December 12, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 38)
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: HD_0344
From
Haemophilus ducreyi [TaxID: 730] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=35000HP / ATCC 700724;
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.;
"The complete genome sequence of Haemophilus ducreyi.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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
AE017143; AAP95319.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_872930.1; -.
3D structure databases
HSSP P32050; 1GU6. [HSSP ENTRY / PDB]
ModBase Q7VNX8.
Enzyme and pathway databases
BioCyc HDUC233412:HD_0344-MON; -.
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).
GO:0055114; Biological process: oxidation reduction (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 Q7VNX8.
Genome annotation databases
GeneID 1490348; -.
GenomeReviews AE017143_GR; HD_0344.
KEGG hdu:HD0344; -.
NMPDR fig|233412.1.peg.295; -.
Phylogenomic databases
HOGENOM Q7VNX8; -.
Genome annotation databases
CMR Q7VNX8; HD_0344.
Other
ProtoNet Q7VNX8.
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    25  25     Potential. 
CHAIN   26   502  477     Cytochrome c-552. PRO_0000268966
METAL   105   105        Iron (heme 3 axial ligand) (By similarity). 
METAL   137   137        Iron (heme 1 axial ligand) (By similarity). 
METAL   175   175        Iron (heme 2 axial ligand) (By similarity). 
METAL   224   224        Iron (heme 3 axial ligand) (By similarity). 
METAL   226   226        Calcium (By similarity). 
METAL   227   227        Calcium (via carbonyl oxygen) (By similarity). 
METAL   271   271        Calcium (via carbonyl oxygen) (By similarity). 
METAL   273   273        Calcium (By similarity). 
METAL   285   285        Iron (heme 5 axial ligand) (By similarity). 
METAL   296   296        Iron (heme 4 axial ligand) (By similarity). 
METAL   311   311        Iron (heme 2 axial ligand) (By similarity). 
METAL   328   328        Iron (heme 5 axial ligand) (By similarity). 
METAL   403   403        Iron (heme 4 axial ligand) (By similarity). 
BINDING   133   133        Heme 1 (covalent) (By similarity). 
BINDING   136   136        Heme 1 (covalent) (By similarity). 
BINDING   171   171        Heme 2 (covalent) (By similarity). 
BINDING   174   174        Heme 2 (covalent) (By similarity). 
BINDING   220   220        Heme 3 (covalent) (By similarity). 
BINDING   223   223        Heme 3 (covalent) (By similarity). 
BINDING   227   227        Substrate (By similarity). 
BINDING   274   274        Substrate (By similarity). 
BINDING   292   292        Heme 4 (covalent) (By similarity). 
BINDING   295   295        Heme 4 (covalent) (By similarity). 
BINDING   324   324        Heme 5 (covalent) (By similarity). 
BINDING   327   327        Heme 5 (covalent) (By similarity). 
Sequence information
Length: 502 AA [This is the length of the unprocessed precursor] Molecular weight: 56641 Da [This is the MW of the unprocessed precursor] CRC64: FF214013B33FDE04 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKYLTKSRVI ATIAMLGCLS VSAWAETPTN QPESLTDKAL KHEKLGVVVE SANHKFAEKY 

        70         80         90        100        110        120 
RLQYDSWKAT AESTDRSSAL EADPRLVVLW AGYAFAKEYN KPRGHYYAVT DVREILRTGA 

       130        140        150        160        170        180 
PKDENDGPQP MACWTCKGPD VPRLIEEKGE RGYFDPKWAK YGAEIVNSIG CADCHDTTSK 

       190        200        210        220        230        240 
AFEEGKPALR VARPHVLRAL ESVGWRFEDL DKHGKRVAVC SNCHVEYYFK DKKDVTFPWA 

       250        260        270        280        290        300 
KGVDVDSIEK YYDESQFTDW THALSKAPML KTQHPDFEVW SQGVHGKNGV TCIDCHMPKV 

       310        320        330        340        350        360 
KDKDGKVYTE HKIGNPFDRF DATCKTCHEQ SKQTLQDRVK EHKAQVKEAM IRLEDQIVKA 

       370        380        390        400        410        420 
HFEAKVAWDA GATAEEMQDI LMAIRHAQWR WDYSAAGHGN HFHAPDVMLH TIATGLDRVA 

       430        440        450        460        470        480 
DARAKLGVVL TKHGVETPIV MPDISTREKA QKAVGIDIAK DQAAKDEFLR TVVPQWERQA 

       490        500 
RERGLLPEVT PKSVTTPKVD AK
Q7VNX8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!