Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q5PJ02 (NRFA_SALPA)

Last modified November 4, 2008. Version 32. 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: SPA4094
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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.

Catalytic activity

NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+).

Cofactor

Binds 1 calcium ion per monomer By similarity.

Binds 5 heme groups covalently per monomer By similarity.

Pathway

Nitrogen metabolism; nitrate reduction (assimilation).

Subcellular location

PeriplasmBy similarity.

Sequence similarities

Belongs to the cytochrome c-552 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 478452Cytochrome c-552
PRO_0000268973

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
Q5PJ02-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 65D3E240FFEA9BA3

FASTA47853,744
        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 ALLIQQEGED GYFHGKWARG GPEIVNDLGC ADCHNTASDD FAQGKPALTL 

       190        200        210        220        230        240 
SRPYAERAME AISKPFDKAG 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 RKNSLLSQ 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

CP000026 Genomic DNA. Translation: AAV79838.1.
RefSeqYP_153150.1.

3D structure databases

SMRQ5PJ02. Positions 38-478.
ModBaseSearch...

Genome annotation databases

GeneID3177712.
GenomeReviewsGene locus SPA4094 in contig CP000026_GR.
KEGGspt:SPA4094.
NMPDRfig|295319.3.peg.4057.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PJ02.

Enzyme and pathway databases

BioCycSENT295319:SPA4094-MON.

Family and domain databases

HAMAPMF_01182.
[Tree]
InterProIPR003321. Cyt_c552.
IPR017570. Cytc_552_NO2Rdtase_formate-dep.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamPF02335. Cytochrom_C552. 1 hit.
[Graphical view]
PIRSFPIRSF000243. Cyt_c552. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNRFA_SALPA
AccessionPrimary (citable) accession number: Q5PJ02
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 4, 2005
Last modified: November 4, 2008
This is version 32 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