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P0AF32 (NARV_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Respiratory nitrate reductase 2 gamma chain

EC=1.7.99.4
Gene names
Name:narV
Ordered Locus Names:b1465, JW1460
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit.

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactor

Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme By similarity.

Subunit structure

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 226226Respiratory nitrate reductase 2 gamma chain
PRO_0000096731

Regions

Topological domain2 – 43Periplasmic By similarity
Transmembrane5 – 3026Helical; Name=1; By similarity
Topological domain31 – 4818Cytoplasmic By similarity
Transmembrane49 – 7123Helical; Name=2; By similarity
Topological domain72 – 8312Periplasmic By similarity
Transmembrane84 – 11330Helical; Name=3; By similarity
Topological domain114 – 12512Cytoplasmic By similarity
Transmembrane126 – 14924Helical; Name=4; By similarity
Topological domain150 – 18334Periplasmic By similarity
Transmembrane184 – 19916Helical; Name=5; By similarity
Topological domain200 – 22627Cytoplasmic By similarity

Sites

Metal binding571Iron (heme B 1 axial ligand) By similarity
Metal binding671Iron (heme B 2 axial ligand) By similarity
Metal binding1881Iron (heme B 2 axial ligand) By similarity
Metal binding2061Iron (heme B 1 axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AF32 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 1D5FAC307F3D5B84

FASTA22626,018
        10         20         30         40         50         60 
MIQYLNVFFY DIYPYICATV FFLGSWLRYD YGQYTWRASS SQMLDKRGMV IWSNLFHIGI 

        70         80         90        100        110        120 
LGIFFGHLFG MLTPHWMYAW FLPVAAKQLM AMVLGGICGV LTLIGGAGLL WRRLTNQRVR 

       130        140        150        160        170        180 
ATSTTPDIII MSILLIQCLL GLSTIPFSAQ YPDGSEMMKL VGWAQSIVTF RGGSSEMLNG 

       190        200        210        220 
VAFVFRLHLV LGMTIFLLFP FTRLVHVWSA PFEYFTRRYQ IVRSRR 

« Hide

References

« Hide 'large scale' references
[1]"Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon."
Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.
Mol. Gen. Genet. 222:104-111(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17110 Genomic DNA. Translation: CAA34967.1.
U00096 Genomic DNA. Translation: AAC74547.1.
AP009048 Genomic DNA. Translation: BAA15102.1.
PIRS11430.
RefSeqNP_415982.1. NC_000913.3.
YP_489730.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AF32.
SMRP0AF32. Positions 3-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b1465.

Protein family/group databases

TCDB5.A.3.1.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74547; AAC74547; b1465.
BAA15102; BAA15102; BAA15102.
GeneID12934343.
946029.
KEGGecj:Y75_p1441.
eco:b1465.
PATRIC32118222. VBIEscCol129921_1531.

Organism-specific databases

EchoBASEEB0638.
EcoGeneEG10644. narV.

Phylogenomic databases

eggNOGCOG2181.
HOGENOMHOG000237376.
KOK00374.
OMAVLFHVGV.
OrthoDBEOG6K13W6.
PhylomeDBP0AF32.
ProtClustDBCLSK880007.

Enzyme and pathway databases

BioCycEcoCyc:NARV-MONOMER.
ECOL316407:JW1460-MONOMER.
MetaCyc:NARV-MONOMER.

Gene expression databases

GenevestigatorP0AF32.

Family and domain databases

InterProIPR023234. NarG-like_domain.
IPR003816. Nitrate_red_gam.
[Graphical view]
PfamPF02665. Nitrate_red_gam. 1 hit.
[Graphical view]
SUPFAMSSF103501. SSF103501. 1 hit.
TIGRFAMsTIGR00351. narI. 1 hit.
ProtoNetSearch...

Other

PROP0AF32.

Entry information

Entry nameNARV_ECOLI
AccessionPrimary (citable) accession number: P0AF32
Secondary accession number(s): P19316
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene