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Reviewed, UniProtKB/Swiss-Prot A6L890 (NRFA_PARD8)

Last modified November 4, 2008. Version 15. 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: BDI_0109
OrganismParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP]
Taxonomic identifier435591 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeParabacteroides

Protein attributes

Sequence length494 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 – 3131 Potential
Chain32 – 494463Cytochrome c-552
PRO_1000065804

Sites

Metal binding1161Iron (heme 3 axial ligand) By similarity
Metal binding1481Iron (heme 1 axial ligand) By similarity
Metal binding1861Iron (heme 2 axial ligand) By similarity
Metal binding2281Iron (heme 3 axial ligand) By similarity
Metal binding2301Calcium By similarity
Metal binding2311Calcium; via carbonyl oxygen By similarity
Metal binding2761Calcium; via carbonyl oxygen By similarity
Metal binding2781Calcium By similarity
Metal binding2901Iron (heme 5 axial ligand) By similarity
Metal binding3011Iron (heme 4 axial ligand) By similarity
Metal binding3151Iron (heme 2 axial ligand) By similarity
Metal binding3321Iron (heme 5 axial ligand) By similarity
Metal binding4071Iron (heme 4 axial ligand) By similarity
Binding site1441Heme 1 (covalent) By similarity
Binding site1471Heme 1 (covalent) By similarity
Binding site1821Heme 2 (covalent) By similarity
Binding site1851Heme 2 (covalent) By similarity
Binding site2241Heme 3 (covalent) By similarity
Binding site2271Heme 3 (covalent) By similarity
Binding site2311Substrate By similarity
Binding site2791Substrate By similarity
Binding site2971Heme 4 (covalent) By similarity
Binding site3001Heme 4 (covalent) By similarity
Binding site3281Heme 5 (covalent) By similarity
Binding site3311Heme 5 (covalent) By similarity

Sequences

Sequence LengthMass (Da)Tools
A6L890-1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 58ECCCF0E077EF53

FASTA49456,145
        10         20         30         40         50         60 
MEKKLKSWQG WLLFGGTMVV VFVLGMIAAS VNERHAEVTS VMNNKKTEIT GIEARNDKFE 

        70         80         90        100        110        120 
SNYPREYQTW EATADTSFKS LYNGNQAVDV LEARPEMVIL WAGYAFSKDY STPRGHMHAI 

       130        140        150        160        170        180 
EDMRNTLRVG APMTENEGPQ PATCWTCKSP DVPRMMQAMG VDNFYKGKWA SLGKEIVNPI 

       190        200        210        220        230        240 
GCADCHEPEN MNLHISRPAL IEAFQRQGKD ITKATQQEMR SLVCAQCHVE YYFKGDGKYL 

       250        260        270        280        290        300 
TFPWDKGSTV EDMEAYYDEA GFADYTHKLS RAPILKAQHP DYEISQMGIH AQRGVSCADC 

       310        320        330        340        350        360 
HMPYKSEGGV KYSDHHIQSP LAMIDRTCQV CHRESEETLR NNVYERQNKA NEMRNRLETE 

       370        380        390        400        410        420 
LAKAHVEAKF AWDKGATEDQ MKDVLKLIRQ AQWRWDFGVA SHGGAFHAPQ EIQRILGNGL 

       430        440        450        460        470        480 
DKAMQARLAT AKVLAKLGYT DDVPMPDFST KEKAQQYIGL DMAAERTAKE KFLNTIVPQW 

       490 
MKEAQENNRL AKNI 

« Hide

References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000140 Genomic DNA. Translation: ABR41904.1.
RefSeqYP_001301526.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5305200.
GenomeReviewsGene locus BDI_0109 in contig CP000140_GR.
KEGGpdi:BDI_0109.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01182.
[Tree]
InterProIPR003321. Cyt_c552.
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_PARD8
AccessionPrimary (citable) accession number: A6L890
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 24, 2007
Last modified: November 4, 2008
This is version 15 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