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UniProtKB/Swiss-Prot entry P0ABK9


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

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Entry information
Entry name NRFA_ECOLI
Primary accession number P0ABK9
Secondary accession numbers P32050 Q2M6N4
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on November 8, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 37)
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: b4070, JW4031
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-42 AND 150-167.
STRAIN=K12;
PubMed=7934939 [NCBI, ExPASy, EBI, Israel, Japan]
Darwin A., Hussain H.A., Griffiths L., Grove J., Sambongi Y., Busby S., Cole J.;
"Regulation and sequence of the structural gene for cytochrome c552 from Escherichia coli: not a hexahaem but a 50 kDa tetrahaem nitrite reductase.";
Mol. Microbiol. 9:1255-1265(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
CHARACTERIZATION AS A CYTOCHROME C.
DOI=10.1016/0378-1097(94)90397-2; PubMed=8039676 [NCBI, ExPASy, EBI, Israel, Japan]
Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., Pommier J., Mejean V., Cole J.A.;
"A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12.";
FEMS Microbiol. Lett. 119:89-94(1994).
[6]
HEME-BINDING, MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-126.
PubMed=9593308 [NCBI, ExPASy, EBI, Israel, Japan]
Eaves D.J., Grove J., Staudenmann W., James P., Poole R.K., White S.A., Griffiths I., Cole J.A.;
"Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli.";
Mol. Microbiol. 28:205-216(1998).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MAGNETIC CIRCULAR DICHROISM, AND EPR SPECTROSCOPY.
DOI=10.1021/bi015765d; PubMed=11863430 [NCBI, ExPASy, EBI, Israel, Japan]
Bamford V.A., Angove H.C., Seward H.E., Thomson A.J., Cole J.A., Butt J.N., Hemmings A.M., Richardson D.J.;
"Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli.";
Biochemistry 41:2921-2931(2002).
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
X72298; CAA51048.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00006; AAC43164.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77040.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78072.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S39590; S39590.
RefSeq AP_004571.1; -.
NP_418494.1; -.
3D structure databases
PDB
1GU6; X-ray; 2.50 A; A/C/E/G=27-478.[ExPASy / RCSB / EBI]
2RDZ; X-ray; 1.74 A; A/B/C/D=27-478.[ExPASy / RCSB / EBI]
2RF7; X-ray; 2.04 A; A/B/C/D=37-477.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GU6; -.
2RDZ; -.
2RF7; -.
ModBase P0ABK9.
Enzyme and pathway databases
BioCyc EcoCyc:CYTOCHROMEC552-MON; -.
Organism-specific databases
EchoBASE EB1729; -.
EcoGene EG11781; nrfA.
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.
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).
Genome annotation databases
GeneID 948571; -.
GenomeReviews AP009048_GR; JW4031.
U00096_GR; b4070.
KEGG ecj:JW4031; -.
eco:b4070; -.
Phylogenomic databases
HOGENOM P0ABK9; -.
Genome annotation databases
CMR P0ABK9; b4070.
Other
ProtoNet P0ABK9.
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    26  26      
CHAIN   27   478  452     Cytochrome c-552. PRO_0000006578
METAL   94    94        Iron (heme 3 axial ligand). 
METAL   126   126        Iron (heme 1 axial ligand). 
METAL   164   164        Iron (heme 2 axial ligand). 
METAL   213   213        Iron (heme 3 axial ligand). 
METAL   215   215        Calcium. 
METAL   216   216        Calcium; via carbonyl oxygen. 
METAL   261   261        Calcium; via carbonyl oxygen. 
METAL   263   263        Calcium. 
METAL   275   275        Iron (heme 5 axial ligand). 
METAL   286   286        Iron (heme 4 axial ligand). 
METAL   301   301        Iron (heme 2 axial ligand). 
METAL   318   318        Iron (heme 5 axial ligand). 
METAL   393   393        Iron (heme 4 axial ligand). 
BINDING   122   122        Heme 1 (covalent). 
BINDING   125   125        Heme 1 (covalent). 
BINDING   160   160        Heme 2 (covalent). 
BINDING   163   163        Heme 2 (covalent). 
BINDING   209   209        Heme 3 (covalent). 
BINDING   212   212        Heme 3 (covalent). 
BINDING   216   216        Substrate (By similarity). 
BINDING   264   264        Substrate (By similarity). 
BINDING   282   282        Heme 4 (covalent). 
BINDING   285   285        Heme 4 (covalent). 
BINDING   314   314        Heme 5 (covalent). 
BINDING   317   317        Heme 5 (covalent). 
MUTAGEN   126   126        K->H,I,L: Almost complete loss of nitrite reductase activity. 
HELIX   42    45  4      
TURN   46    48  3      
HELIX   50    57  8      
HELIX   58    61  4      
HELIX   68    71  4      
HELIX   74    78  5      
TURN   79    81  3      
HELIX   83    85  3      
HELIX   94    96  3      
HELIX   97   103  7      
HELIX   105   107  3      
STRAND   116   119  4      
HELIX   120   123  4      
TURN   124   126  3      
HELIX   129   137  9      
HELIX   139   143  5      
STRAND   144   146  3      
HELIX   147   150  4      
TURN   151   153  3      
HELIX   160   163  4      
HELIX   169   172  4      
HELIX   183   191  9      
HELIX   196   198  3      
HELIX   201   209  9      
TURN   210   212  3      
STRAND   217   219  3      
TURN   220   223  4      
STRAND   224   226  3      
HELIX   235   244  10      
STRAND   249   251  3      
TURN   253   255  3      
HELIX   266   272  7      
HELIX   274   277  4      
HELIX   282   286  5      
STRAND   289   291  3      
STRAND   297   299  3      
HELIX   306   312  7      
HELIX   314   316  3      
HELIX   322   359  38      
HELIX   364   385  22      
HELIX   390   393  4      
HELIX   395   422  28      
HELIX   437   443  7      
HELIX   448   472  25      
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 53703 Da [This is the MW of the unprocessed precursor] CRC64: F965E986412A0456 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTRIKINARR IFSLLIPFFF FTSVHAEQTA APAKPVTVEA KNETFAPQHP DQYLSWKATS 

        70         80         90        100        110        120 
EQSERVDALA EDPRLVILWA GYPFSRDYNK PRGHAFAVTD VRETLRTGAP KNAEDGPLPM 

       130        140        150        160        170        180 
ACWSCKSPDV ARLIQKDGED GYFHGKWARG GPEIVNNLGC ADCHNTASPE FAKGKPELTL 

       190        200        210        220        230        240 
SRPYAARAME AIGKPFEKAG RFDQQSMVCG QCHVEYYFDG KNKAVKFPWD DGMKVENMEQ 

       250        260        270        280        290        300 
YYDKIAFSDW TNSLSKTPML KAQHPEYETW TAGIHGKNNV TCIDCHMPKV QNAEGKLYTD 

       310        320        330        340        350        360 
HKIGNPFDNF AQTCANCHTQ DKAALQKVVA ERKQSINDLK IKVEDQLVHA HFEAKAALDA 

       370        380        390        400        410        420 
GATEAEMKPI QDDIRHAQWR WDLAIASHGI HMHAPEEGLR MLGTAMDKAA DARTKLARLL 

       430        440        450        460        470 
ATKGITHEIQ IPDISTKEKA QQAIGLNMEQ IKAEKQDFIK TVIPQWEEQA RKNGLLSQ 

P0ABK9 in FASTA format

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