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Reviewed, UniProtKB/Swiss-Prot Q9Z4P4 (NRFA_SULDE)

Last modified October 13, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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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
OrganismSulfurospirillum deleyianum
Taxonomic identifier65553 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Sulfurospirillum

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Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays a role in nitrite reduction. HAMAP MF_01182

Catalytic activity

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

Cofactor

Binds 1 calcium ion per monomer. HAMAP MF_01182

Binds 5 heme groups covalently per monomer. Ref.2

Pathway

Nitrogen metabolism; nitrate reduction (assimilation). HAMAP MF_01182

Subunit structure

Homodimer. May also exist as a membrane-associated heterooligomeric complex. Ref.2

Subcellular location

Periplasm. HAMAP MF_01182

Miscellaneous

X-ray crystallographic analysis includes a sulfate ion that is thought to be at the substrate binding site. HAMAP MF_01182

Sequence similarities

Belongs to the cytochrome c-552 family.

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Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

nitrogen compound metabolic process

Inferred from electronic annotation. Source: HAMAP

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

heme binding

Inferred from electronic annotation. Source: InterPro

nitrite reductase (cytochrome, ammonia-forming) activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 HAMAP MF_01182
Chain22 – 514493Cytochrome c-552 HAMAP MF_01182
PRO_0000006583

Sites

Metal binding1011Iron (heme 3 axial ligand) HAMAP MF_01182
Metal binding1331Iron (heme 1 axial ligand) HAMAP MF_01182
Metal binding1711Iron (heme 2 axial ligand) HAMAP MF_01182
Metal binding2141Iron (heme 3 axial ligand) HAMAP MF_01182
Metal binding2161Calcium HAMAP MF_01182
Metal binding2171Calcium; via carbonyl oxygen HAMAP MF_01182
Metal binding2801Calcium; via carbonyl oxygen HAMAP MF_01182
Metal binding2811Calcium HAMAP MF_01182
Metal binding2931Iron (heme 5 axial ligand) HAMAP MF_01182
Metal binding3041Iron (heme 4 axial ligand) HAMAP MF_01182
Metal binding3181Iron (heme 2 axial ligand) HAMAP MF_01182
Metal binding3361Iron (heme 5 axial ligand) HAMAP MF_01182
Metal binding4111Iron (heme 4 axial ligand) HAMAP MF_01182
Binding site1291Heme 1 (covalent) HAMAP MF_01182
Binding site1321Heme 1 (covalent) HAMAP MF_01182
Binding site1671Heme 2 (covalent) HAMAP MF_01182
Binding site1701Heme 2 (covalent) HAMAP MF_01182
Binding site2101Heme 3 (covalent) HAMAP MF_01182
Binding site2131Heme 3 (covalent) HAMAP MF_01182
Binding site2171Substrate HAMAP MF_01182
Binding site2821Substrate HAMAP MF_01182
Binding site3001Heme 4 (covalent) HAMAP MF_01182
Binding site3031Heme 4 (covalent) HAMAP MF_01182
Binding site3321Heme 5 (covalent) HAMAP MF_01182
Binding site3351Heme 5 (covalent) HAMAP MF_01182

Secondary structure

1 ....................................................................................... 514
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9Z4P4-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E63C119D4FA98562

FASTA51457,611
        10         20         30         40         50         60 
MKFKLLLAGS LVAVGAMALL ASNINEKEKQ RVELAKAPSE AGIAGKEKSE EWAKYYPRQF 

        70         80         90        100        110        120 
DSWKKTKEYD SFTDMLAKDP ALVIAWSGYA FSKDYNSPRG HYYALQDNVN SLRTGAPVDA 

       130        140        150        160        170        180 
KTGPLPTACW TCKSPDVPRL IEEDGELEYF TGKWAKYGSQ IVNVIGCANC HDDKTAELKV 

       190        200        210        220        230        240 
RVPHLNRGLQ AAGLKTFEES THQDKRTLVC AQCHVEYYFK KTEWKDAKGA DKTAMVVTLP 

       250        260        270        280        290        300 
WANGVGKDGN AGVEGMIKYY DEINFSDWTH NISKTPMLKA QHPGFEFWKS GIHGQKGVSC 

       310        320        330        340        350        360 
ADCHMPYTQE GSVKYSDHQV KENPLDSMDQ SCMNCHRESE SKLRGIVHQK YERKEFLNKV 

       370        380        390        400        410        420 
AFDNIGKAHL ETGKAIEAGA SDEELKEVRK LIRHGQFKAD MAIAAHGNYF HAPEETLRLL 

       430        440        450        460        470        480 
AAGSDDAQKA RLLLVKILAK HGVMDYIAPD FDTKDKAQKL AKVDIAALAA EKMKFKQTLE 

       490        500        510 
QEWKKEAKAK GRANPELYKD VDTINDGKSS WNKK

« Hide

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References

[1]"Structure of cytochrome c nitrite reductase."
Einsle O., Messerschmidt A., Stach P., Bourenkov G.P., Bartunik H.D., Huber R., Kroneck P.M.H.
Nature 400:476-480(1999) [PubMed: 10440380] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[2]"Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties."
Schumacher W., Hole U., Kroneck P.M.H.
Biochem. Biophys. Res. Commun. 205:911-916(1994) [PubMed: 7999130] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT, HEME-BINDING.

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Cross-references

Sequence databases

AJ133037 mRNA. Translation: CAB37320.2. Different initiation.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QDBX-ray1.90A/B/C42-514[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.7.2.2. 191626.

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...

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Entry information

Entry nameNRFA_SULDE
AccessionPrimary (citable) accession number: Q9Z4P4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: October 13, 2009
This is version 71 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)

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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

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