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UniProtKB/Swiss-Prot entry A8A7H1

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

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Entry information
Entry name NRFA_ECOHS
Primary accession number A8A7H1
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 23, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 12)
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: EcHS_A4315
From
Escherichia coli O9:H4 (strain HS) [TaxID: 331112] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00619-08; PubMed=18676672 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.;
"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates.";
J. Bacteriol. 190:6881-6893(2008).
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
CP000802; ABV08475.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001460858.1; -.
3D structure databases
ModBase A8A7H1.
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).
ProtoNet A8A7H1.
Genome annotation databases
GeneID 5591369; -.
GenomeReviews CP000802_GR; EcHS_A4315.
KEGG ecx:EcHS_A4315; -.
CMR A8A7H1; EcHS_A4315.
Other
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_1000065802
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: 53708 Da [This is the MW of the unprocessed precursor] CRC64: B02F5CE597EABFEE [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTRIKINARR IFSLLIPFFF FTSVHAEQTA APAKTVTVEA 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 
ATKGITHEIE IPDISTKEKA QQAIGLNMEQ IKAEKQDFIK TVIPQWEEQA RKNGLLSQ
A8A7H1 in FASTA format

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