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P19318 (NARY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Respiratory nitrate reductase 2 beta chain

EC=1.7.99.4
Gene names
Name:narY
Ordered Locus Names:b1467, JW1462
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length514 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 beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactor

Binds 3 4Fe-4S clusters per subunit By similarity.

Binds 1 3Fe-4S cluster per subunit 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 membrane; Peripheral membrane protein.

Sequence similarities

Contains 3 4Fe-4S ferredoxin-type domains.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Respiratory nitrate reductase 2 beta chain
PRO_0000096734

Regions

Domain7 – 35294Fe-4S ferredoxin-type 1
Domain174 – 205324Fe-4S ferredoxin-type 2
Domain207 – 236304Fe-4S ferredoxin-type 3

Sites

Metal binding161Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding191Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding221Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding261Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1831Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1861Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1911Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1951Iron-sulfur 4 (3Fe-4S) By similarity
Metal binding2161Iron-sulfur 4 (3Fe-4S) By similarity
Metal binding2221Iron-sulfur 4 (3Fe-4S) By similarity
Metal binding2261Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2431Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2461Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2581Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2621Iron-sulfur 1 (4Fe-4S) By similarity

Experimental info

Sequence conflict325 – 3262QR → HG in CAA34965. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19318 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 82D997DB093CD818

FASTA51458,558
        10         20         30         40         50         60 
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TGREGMEYAW FNNVETKPGI GYPKNWEDQE 

        70         80         90        100        110        120 
EWQGGWVRDV NGKIRPRLGN KMGVITKIFA NPVVPQIDDY YEPFTFDYEH LHSAPEGKHI 

       130        140        150        160        170        180 
PTARPRSLID GKRMDKVIWG PNWEELLGGE FEKRARDRNF EAMQKEMYGQ FENTFMMYLP 

       190        200        210        220        230        240 
RLCEHCLNPS CVATCPSGAI YKREEDGIVL IDQDKCRGWR LCISGCPYKK IYFNWKSGKS 

       250        260        270        280        290        300 
EKCIFCYPRI ESGQPTVCSE TCVGRIRYLG VLLYDADRIE EAASTEREVD LYERQCEVFL 

       310        320        330        340        350        360 
DPHDPSVIEE ALKQGIPQNV IDAAQRSPVY KMAMDWKLAL PLHPEYRTLP MVWYVPPLSP 

       370        380        390        400        410        420 
IQSYADAGGL PKSEGVLPAI ESLRIPVQYL ANMLSAGDTG PVLRALKRMM AMRHYMRSQT 

       430        440        450        460        470        480 
VEGVTDTRAI DEVGLSVAQV EEMYRYLAIA NYEDRFVIPT SHREMAGDAF AERNGCGFTF 

       490        500        510 
GDGCHGSDSK FNLFNSSRID AINITEVRDK AEGE 

« 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], PROTEIN SEQUENCE OF 1-18.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17110 Genomic DNA. Translation: CAA34965.1.
U00096 Genomic DNA. Translation: AAC74549.1.
AP009048 Genomic DNA. Translation: BAA15104.1.
PIRF64899.
RefSeqNP_415984.1. NC_000913.3.
YP_489732.1. NC_007779.1.

3D structure databases

ProteinModelPortalP19318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10323N.
IntActP19318. 14 interactions.
MINTMINT-1251788.
STRING511145.b1467.

Protein family/group databases

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

Proteomic databases

PaxDbP19318.
PRIDEP19318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74549; AAC74549; b1467.
BAA15104; BAA15104; BAA15104.
GeneID12933900.
946034.
KEGGecj:Y75_p1443.
eco:b1467.
PATRIC32118226. VBIEscCol129921_1533.

Organism-specific databases

EchoBASEEB0641.
EcoGeneEG10647. narY.

Phylogenomic databases

eggNOGCOG1140.
HOGENOMHOG000237353.
KOK00371.
OMAKRMDKIV.
OrthoDBEOG6X3W4C.
PhylomeDBP19318.

Enzyme and pathway databases

BioCycEcoCyc:NARY-MONOMER.
ECOL316407:JW1462-MONOMER.
MetaCyc:NARY-MONOMER.

Gene expression databases

GenevestigatorP19318.

Family and domain databases

Gene3D1.10.3650.10. 1 hit.
InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR029263. Nitr_red_bet_C.
IPR006547. NO3_Rdtase_bsu.
[Graphical view]
PfamPF13247. Fer4_11. 1 hit.
PF14711. Nitr_red_bet_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR01660. narH. 1 hit.
PROSITEPS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

PROP19318.

Entry information

Entry nameNARY_ECOLI
AccessionPrimary (citable) accession number: P19318
Secondary accession number(s): P78267
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

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