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Reviewed, UniProtKB/Swiss-Prot A7ZUU5 (NRFA_ECO24)

Last modified February 9, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytochrome c-552
    EC=1.7.2.2
Alternative name(s):
    Ammonia-forming cytochrome c nitrite reductase
      Short name=Cytochrome c nitrite reductase
Gene names
Name: nrfA
Ordered Locus Names: EcE24377A_4626
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays a role in nitrite reduction By similarity. HAMAP MF_01182

Catalytic activity

NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+. HAMAP MF_01182

Cofactor

Binds 1 calcium ion per monomer By similarity. HAMAP MF_01182

Binds 5 heme groups covalently per monomer By similarity. HAMAP MF_01182

Pathway

Nitrogen metabolism; nitrate reduction (assimilation). HAMAP MF_01182

Subcellular location

Periplasm By similarity HAMAP MF_01182.

Sequence similarities

Belongs to the cytochrome c-552 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 478452Cytochrome c-552 HAMAP MF_01182
PRO_1000065801

Sites

Metal binding941Iron (heme 3 axial ligand) By similarity
Metal binding1261Iron (heme 1 axial ligand) By similarity
Metal binding1641Iron (heme 2 axial ligand) By similarity
Metal binding2131Iron (heme 3 axial ligand) By similarity
Metal binding2151Calcium By similarity
Metal binding2161Calcium; via carbonyl oxygen By similarity
Metal binding2611Calcium; via carbonyl oxygen By similarity
Metal binding2631Calcium By similarity
Metal binding2751Iron (heme 5 axial ligand) By similarity
Metal binding2861Iron (heme 4 axial ligand) By similarity
Metal binding3011Iron (heme 2 axial ligand) By similarity
Metal binding3181Iron (heme 5 axial ligand) By similarity
Metal binding3931Iron (heme 4 axial ligand) By similarity
Binding site1221Heme 1 (covalent) By similarity
Binding site1251Heme 1 (covalent) By similarity
Binding site1601Heme 2 (covalent) By similarity
Binding site1631Heme 2 (covalent) By similarity
Binding site2091Heme 3 (covalent) By similarity
Binding site2121Heme 3 (covalent) By similarity
Binding site2161Substrate By similarity
Binding site2641Substrate By similarity
Binding site2821Heme 4 (covalent) By similarity
Binding site2851Heme 4 (covalent) By similarity
Binding site3141Heme 5 (covalent) By similarity
Binding site3171Heme 5 (covalent) By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZUU5-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: F965E986412A0456

FASTA47853,703
        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 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
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.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV19042.1.
RefSeqYP_001465574.1.

3D structure databases

SMRA7ZUU5. Positions 37-477.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZUU5.

Proteomic databases

PRIDEA7ZUU5.

Genome annotation databases

GeneID5586873.
GenomeReviewsGene locus EcE24377A_4626 in contig CP000800_GR.
KEGGecw:EcE24377A_4626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3303.
HOGENOMHBG488281.
OMAPWDMGTT.

Family and domain databases

HAMAPMF_01182. Cytochrom_C552.
[Tree]
InterProIPR003321. Cyt_c552.
IPR017570. Cyt_c_NO2Rdtase_formate-dep.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamPF02335. Cytochrom_C552. 1 hit.
[Graphical view]
PIRSFPIRSF000243. Cyt_c552. 1 hit.
TIGRFAMsTIGR03152. cyto_c552_HCOOH. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNRFA_ECO24
AccessionPrimary (citable) accession number: A7ZUU5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: February 9, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents