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Q9S1E5 (NRFA_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:WS0969
OrganismWolinella succinogenes [Complete proteome] [HAMAP]
Taxonomic identifier844 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Wolinella

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in nitrite reduction. Ref.1

Catalytic activity

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

Cofactor

Binds 1 calcium ion per monomer.

Binds 5 heme groups covalently per monomer.

Pathway

Nitrogen metabolism; nitrate reduction (assimilation). HAMAP MF_01182

Subunit structure

Heterodimer with NrfH. Ref.1

Subcellular location

Periplasm Ref.1.

Miscellaneous

X-ray crystallographic determinations include sulfate or azide ions at what is thought to be the substrate binding site. HAMAP MF_01182

Sequence similarities

Belongs to the cytochrome c-552 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1
Chain23 – 507485Cytochrome c-552 HAMAP MF_01182
PRO_0000006584

Sites

Metal binding1021Iron (heme 3 axial ligand)
Metal binding1341Iron (heme 1 axial ligand)
Metal binding1721Iron (heme 2 axial ligand)
Metal binding2151Iron (heme 3 axial ligand)
Metal binding2171Calcium
Metal binding2181Calcium; via carbonyl oxygen
Metal binding2741Calcium; via carbonyl oxygen
Metal binding2761Calcium
Metal binding2881Iron (heme 5 axial ligand)
Metal binding2991Iron (heme 4 axial ligand)
Metal binding3131Iron (heme 2 axial ligand)
Metal binding3301Iron (heme 5 axial ligand)
Metal binding4051Iron (heme 4 axial ligand)
Binding site1301Heme 1 (covalent)
Binding site1331Heme 1 (covalent)
Binding site1681Heme 2 (covalent)
Binding site1711Heme 2 (covalent)
Binding site2111Heme 3 (covalent)
Binding site2141Heme 3 (covalent)
Binding site2181Substrate
Binding site2771Substrate
Binding site2951Heme 4 (covalent)
Binding site2981Heme 4 (covalent)
Binding site3261Heme 5 (covalent)
Binding site3291Heme 5 (covalent)

Experimental info

Sequence conflict451E → K in CAB53160. Ref.1

Secondary structure

1 ..................................................................................... 507
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9S1E5 [UniParc].

Last modified September 26, 2003. Version 2.
Checksum: D5CE7E841E3E7AB3

FASTA50757,511
        10         20         30         40         50         60 
MTKFKLLLAG SLVAIVSMGL LASNINEREK ERVALNKTAH SQGIEGKAMS EEWARYYPRQ 

        70         80         90        100        110        120 
FDSWKKTKES DNITDMLKEK PALVVAWAGY PFSKDYNAPR GHYYALQDNI NTLRTGAPVD 

       130        140        150        160        170        180 
GKTGPLPSAC WTCKSPDVPR IIEQDGELEY FTGKWAKYGD EIVNTIGCYN CHDDKSAELK 

       190        200        210        220        230        240 
SKVPYLDRGL SAAGFKTFAE STHQEKRSLV CAQCHVEYYF KKTEWKDDKG VDKTAMVVTL 

       250        260        270        280        290        300 
PWSKGISTEQ MEAYYDEINF ADWTHGISKT PMLKAQHPDW ELYKTGIHGQ KGVSCADCHM 

       310        320        330        340        350        360 
PYTQEGAVKY SDHKVGNPLD NMDKSCMNCH RESEQKLKDI VKQKFERKEF LQDIAFDNIG 

       370        380        390        400        410        420 
KAHLETGKAM ELGATDAELK EIRTHIRHAQ WRADMAIAGH GSFFHAPEEV LRLLASGNEE 

       430        440        450        460        470        480 
AQKARIKLVK VLAKYGAIDY VAPDFETKEK AQKLAKVDME AFIAEKLKFK QTLEQEWKKQ 

       490        500 
AIAKGRLNPE SLKGVDEKSS YYDKTKK

« Hide

References

« Hide 'large scale' references
[1]"A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes."
Simon J., Gross R., Einsle O., Kroneck P.M.H., Kroeger A., Klimmek O.
Mol. Microbiol. 35:686-696(2000) [PubMed: 10672190] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-30, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[2]"Complete genome sequence and analysis of Wolinella succinogenes."
Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C.
Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003) [PubMed: 14500908] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSMZ 1740.
[3]"Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs."
Einsle O., Stach P., Messerschmidt A., Simon J., Kroeger A., Huber R., Kroneck P.M.H.
J. Biol. Chem. 275:39608-39616(2000) [PubMed: 10984487] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 37-507.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ245540 Genomic DNA. Translation: CAB53160.1.
BX571659 Genomic DNA. Translation: CAE10072.1.
RefSeqNP_907172.1. NC_005090.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FS7X-ray1.60A23-507[»]
1FS8X-ray1.60A23-507[»]
1FS9X-ray2.00A1-507[»]
2E80X-ray1.60A23-507[»]
2E81X-ray2.00A23-507[»]
3BNFX-ray1.70A23-507[»]
3BNGX-ray1.50A23-507[»]
3BNHX-ray1.75A23-507[»]
3BNJX-ray1.30A23-507[»]
ProteinModelPortalQ9S1E5.
SMRQ9S1E5. Positions 37-507.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2555567.
GenomeReviewsGene locus WS0969 in contig BX571656_GR.
KEGGwsu:WS0969.
NMPDRfig|273121.1.peg.899.
PATRIC24038988. VBIWolSuc63014_0916.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG488281.
OMACGQCHAS.
ProtClustDBPRK11125.

Enzyme and pathway databases

BioCycWSUC273121:WS0969-MONOMER.

Family and domain databases

HAMAPMF_01182. Cytochrom_C552.
[Tree]
InterProIPR003321. Cyt_c552.
IPR017570. Cyt_c_NO2Rdtase_formate-dep.
IPR011031. Multihaem_cyt.
[Graphical view]
KOK03385.
PfamPF02335. Cytochrom_C552. 1 hit.
[Graphical view]
PIRSFPIRSF000243. Cyt_c552. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNRFA_WOLSU
AccessionPrimary (citable) accession number: Q9S1E5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: September 26, 2003
Last modified: January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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