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Reviewed, UniProtKB/Swiss-Prot Q7MTW1 (NRFA_PORGI)

Last modified January 19, 2010. Version 50. 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: PG_1820
OrganismPorphyromonas gingivalis (Bacteroides gingivalis) [Complete proteome] [HAMAP]
Taxonomic identifier837 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length498 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 – 3131 Potential
Chain32 – 498467Cytochrome c-552 HAMAP MF_01182
PRO_0000268971

Sites

Metal binding1191Iron (heme 3 axial ligand) By similarity
Metal binding1521Iron (heme 1 axial ligand) By similarity
Metal binding1901Iron (heme 2 axial ligand) By similarity
Metal binding2321Iron (heme 3 axial ligand) By similarity
Metal binding2341Calcium By similarity
Metal binding2351Calcium; via carbonyl oxygen By similarity
Metal binding2801Calcium; via carbonyl oxygen By similarity
Metal binding2821Calcium By similarity
Metal binding2941Iron (heme 5 axial ligand) By similarity
Metal binding3051Iron (heme 4 axial ligand) By similarity
Metal binding3191Iron (heme 2 axial ligand) By similarity
Metal binding3361Iron (heme 5 axial ligand) By similarity
Metal binding4111Iron (heme 4 axial ligand) By similarity
Binding site1481Heme 1 (covalent) By similarity
Binding site1511Heme 1 (covalent) By similarity
Binding site1861Heme 2 (covalent) By similarity
Binding site1891Heme 2 (covalent) By similarity
Binding site2281Heme 3 (covalent) By similarity
Binding site2311Heme 3 (covalent) By similarity
Binding site2351Substrate By similarity
Binding site2831Substrate By similarity
Binding site3011Heme 4 (covalent) By similarity
Binding site3041Heme 4 (covalent) By similarity
Binding site3321Heme 5 (covalent) By similarity
Binding site3351Heme 5 (covalent) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7MTW1-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 05F2E38D4AC2E4E0

FASTA49857,267
        10         20         30         40         50         60 
MKNKERKLKS WQGWLIFSSS MVVVFCLGLL AASVTERRAE IQSIYANKKD KIAPFEARNE 

        70         80         90        100        110        120 
MYRGNYPREY ETWTYTADTS FRSEFNGSQA IDVLEQRPNM VIFWAGYAFS RDYTSPRGHM 

       130        140        150        160        170        180 
HAIQDMQRTL RTGNPGIDGA GDMQPATCWV CKSPDVPRMM QAIGVDEFYK NKWSSLGSDI 

       190        200        210        220        230        240 
VNPIGCADCH DPETMDLHIS RPALIEAFQR RGLDITKASH QEMRSLVCAQ CHVEYYFKGE 

       250        260        270        280        290        300 
GKYLTFPWDK GMTMEDAERY YDEAEYYDYI HTLSRAPILK AQHPDFEISQ HGIHAQRGVS 

       310        320        330        340        350        360 
CADCHMPYIS EGGVKFSDHH ITSPLAHMDR TCQTCHRESE EELRKNVYER QRKANEVRNQ 

       370        380        390        400        410        420 
LENELAKAHL EAQFAWDKGA TEKEMTPILK YIRQSQWRWD YGVASHGASF HAPQEITRIL 

       430        440        450        460        470        480 
SNGLERAMQA RIEIARVLAR HGYTDEVPLP DVSTKEKAQK YIGLDMDGLH KNKEKFLETV 

       490 
VPKWVKKAKG KGLLIAAK 

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References

[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed: 12949112] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015924 Genomic DNA. Translation: AAQ66818.1.
RefSeqNP_905919.1.

3D structure databases

HSSPHSSP built from PDB template 1FS7 based on UniProtKB Q9S1E5.
SMRQ7MTW1. Positions 54-496.
ModBaseSearch...

Genome annotation databases

GeneID2551461.
GenomeReviewsGene locus PG_1820 in contig AE015924_GR.
KEGGpgi:PG1820.
NMPDRfig|242619.1.peg.1560.
TIGRPG_1820.

Phylogenomic databases

HOGENOMHBG488281.
OMAPWDMGTT.

Enzyme and pathway databases

BioCycPGIN242619:PG_1820-MONOMER.
BRENDA1.7.2.2. 18777.

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.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNRFA_PORGI
AccessionPrimary (citable) accession number: Q7MTW1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 15, 2003
Last modified: January 19, 2010
This is version 50 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