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UniProtKB/Swiss-Prot entry Q57GV0

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

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Entry information
Entry name NRFA_SALCH
Primary accession number Q57GV0
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on May 10, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 27)
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: SCH_4156
From
Salmonella choleraesuis [TaxID: 591] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC-B67;
DOI=10.1093/nar/gki297; PubMed=15781495 [NCBI, ExPASy, EBI, Israel, Japan]
Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.;
"The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen.";
Nucleic Acids Res. 33:1690-1698(2005).
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
AE017220; AAX68062.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_219143.1; -.
3D structure databases
SMR Q57GV0; 38-478.
ModBase Q57GV0.
Enzyme and pathway databases
BioCyc SENT321314:SCH_4156-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).
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 Q57GV0.
Genome annotation databases
GeneID 3336702; -.
GenomeReviews AE017220_GR; SCH_4156.
KEGG sec:SC4156; -.
NMPDR fig|321314.4.peg.4071; -.
Phylogenomic databases
HOGENOM Q57GV0; -.
Genome annotation databases
CMR Q57GV0; SCH_4156.
Other
ProtoNet Q57GV0.
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    26  26     Potential. 
CHAIN   27   478  452     Cytochrome c-552. PRO_0000268972
METAL   94    94        Iron (heme 3 axial ligand) (By similarity). 
METAL   126   126        Iron (heme 1 axial ligand) (By similarity). 
METAL   164   164        Iron (heme 2 axial ligand) (By similarity). 
METAL   213   213        Iron (heme 3 axial ligand) (By similarity). 
METAL   215   215        Calcium (By similarity). 
METAL   216   216        Calcium; via carbonyl oxygen (By similarity). 
METAL   261   261        Calcium; via carbonyl oxygen (By similarity). 
METAL   263   263        Calcium (By similarity). 
METAL   275   275        Iron (heme 5 axial ligand) (By similarity). 
METAL   286   286        Iron (heme 4 axial ligand) (By similarity). 
METAL   301   301        Iron (heme 2 axial ligand) (By similarity). 
METAL   318   318        Iron (heme 5 axial ligand) (By similarity). 
METAL   393   393        Iron (heme 4 axial ligand) (By similarity). 
BINDING   122   122        Heme 1 (covalent) (By similarity). 
BINDING   125   125        Heme 1 (covalent) (By similarity). 
BINDING   160   160        Heme 2 (covalent) (By similarity). 
BINDING   163   163        Heme 2 (covalent) (By similarity). 
BINDING   209   209        Heme 3 (covalent) (By similarity). 
BINDING   212   212        Heme 3 (covalent) (By similarity). 
BINDING   216   216        Substrate (By similarity). 
BINDING   264   264        Substrate (By similarity). 
BINDING   282   282        Heme 4 (covalent) (By similarity). 
BINDING   285   285        Heme 4 (covalent) (By similarity). 
BINDING   314   314        Heme 5 (covalent) (By similarity). 
BINDING   317   317        Heme 5 (covalent) (By similarity). 
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 53741 Da [This is the MW of the unprocessed precursor] CRC64: 60388EA3D21124C7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MARKTLRARR FFSLIFPFFF ITSVYAEQTP VSAKTVTVEA KNETFAPQHP DQYQSWKATS 

        70         80         90        100        110        120 
EQSAREDALA EDPRLVILWA GYPFSRDYNK PRGHAYAVTD VRETLRTGAP KTAEDGPLPM 

       130        140        150        160        170        180 
ACWSCKSPDV ARLIQQEGED GYFHGKWARG GPEIVNDLGC ADCHNTASDD FAQGKPALTL 

       190        200        210        220        230        240 
SRPYAERAME AIGKPFEKAG RFDQQSMVCG QCHVEYYFDG KNKAVKFPWD EGMKVENMEQ 

       250        260        270        280        290        300 
YYDAIAFSDW TNSLSKTPML KAQHPEYETW SAGIHGKNNV TCIDCHMPKV QNAEGKLYTD 

       310        320        330        340        350        360 
HKIGNPFDNF AQTCANCHTQ DKASLQKVVA ERKQAIHDLK IKVEDQLVHA HFEAKAAWDA 

       370        380        390        400        410        420 
GATDAEMKPI LNDIRHAQWR WDLAIASHGI HMHAPEEGLR MLGSAMDKAA DARTKLARLL 

       430        440        450        460        470 
ATKGITHEIP LPDISTKEKA QKAIGLNMQQ INAEKQDFLK TVVPQWEDQA RKNGLLSQ
Q57GV0 in FASTA format

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