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P11349 (NARH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

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

Names and origin

Protein namesRecommended name:
Respiratory nitrate reductase 1 beta chain

EC=1.7.99.4
Alternative name(s):
Nitrate reductase A subunit beta
Quinol-nitrate oxidoreductase subunit beta
Gene names
Name:narH
Ordered Locus Names:b1225, JW1216
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The nitrate reductase enzyme complex 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.

Binds 1 3Fe-4S cluster per subunit.

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.

Induction

By nitrate.

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

narGP0915211EBI-555067,EBI-547248
narZP193194EBI-555067,EBI-547262

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512Respiratory nitrate reductase 1 beta chain
PRO_0000096720

Regions

Domain7 – 35294Fe-4S ferredoxin-type 1
Domain175 – 206324Fe-4S ferredoxin-type 2
Domain208 – 237304Fe-4S ferredoxin-type 3

Sites

Metal binding161Iron-sulfur 1 (4Fe-4S)
Metal binding191Iron-sulfur 1 (4Fe-4S)
Metal binding221Iron-sulfur 1 (4Fe-4S)
Metal binding261Iron-sulfur 2 (4Fe-4S)
Metal binding1841Iron-sulfur 3 (4Fe-4S)
Metal binding1871Iron-sulfur 3 (4Fe-4S)
Metal binding1921Iron-sulfur 3 (4Fe-4S)
Metal binding1961Iron-sulfur 4 (3Fe-4S)
Metal binding2171Iron-sulfur 4 (3Fe-4S)
Metal binding2231Iron-sulfur 4 (3Fe-4S)
Metal binding2271Iron-sulfur 3 (4Fe-4S)
Metal binding2441Iron-sulfur 2 (4Fe-4S)
Metal binding2471Iron-sulfur 2 (4Fe-4S)
Metal binding2591Iron-sulfur 2 (4Fe-4S)
Metal binding2631Iron-sulfur 1 (4Fe-4S)

Experimental info

Sequence conflict398 – 41720DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195. Ref.6

Secondary structure

.................................................................................................. 512
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11349 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 2E7719C8D078BAEA

FASTA51258,066
        10         20         30         40         50         60 
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE 

        70         80         90        100        110        120 
KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS 

       130        140        150        160        170        180 
QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL 

       190        200        210        220        230        240 
PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK 

       250        260        270        280        290        300 
SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 

       310        320        330        340        350        360 
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS 

       370        380        390        400        410        420 
PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET 

       430        440        450        460        470        480 
VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF 

       490        500        510 
GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP 

« Hide

References

« Hide 'large scale' references
[1]"Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer."
Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.
Mol. Gen. Genet. 218:249-256(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / TG1.
[2]Blasco F.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 398-417.
Strain: K12 / TG1.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"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.
[5]"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.
[6]"narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes."
Sodergren E.J., Demoss J.A.
J. Bacteriol. 170:1721-1729(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-512.
[7]"Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli."
Sodergren E.J., Hsu P.Y., Demoss J.A.
J. Biol. Chem. 263:16156-16162(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.
[8]"EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism."
Guigliarelli B., Asso M., More C., Augier V., Blasco F., Pommier J., Giordano G., Bertrand P.
Eur. J. Biochem. 207:61-68(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[9]"Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes."
Augier V., Guigliarelli B., Asso M., Bertrand P., Frixon C., Giordano G., Chippaux M., Blasco F.
Biochemistry 32:2013-2023(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[10]"Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes."
Augier V., Asso M., Guigliarelli B., More C., Bertrand P., Santini C.-L., Blasco F., Chippaux M., Giordano G.
Biochemistry 32:5099-5108(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[11]"Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters."
Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C., Giordano G., Blasco F.
Biochemistry 35:4828-4836(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[12]"The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters."
Rothery R.A., Magalon A., Giordano G., Guigliarelli B., Blasco F., Weiner J.H.
J. Biol. Chem. 273:7462-7469(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: EPR SPECTROSCOPY, REDOX POTENTIOMETRY OF IRON-SULFUR CLUSTERS.
[13]"Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[14]"Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
Jormakka M., Richardson D., Byrne B., Iwata S.
Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-512.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20147 Genomic DNA. Translation: AAA24195.1.
U00096 Genomic DNA. Translation: AAC74309.1.
AP009048 Genomic DNA. Translation: BAA36095.1.
X16181 Genomic DNA. Translation: CAA34304.1.
PIRRDECNB. F64869.
RefSeqNP_415743.1. NC_000913.3.
YP_489495.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90B1-512[»]
1R27X-ray2.00B/D1-512[»]
1SIWX-ray2.20B1-512[»]
1Y4ZX-ray2.00B1-512[»]
1Y5IX-ray1.90B1-512[»]
1Y5LX-ray2.50B1-512[»]
1Y5NX-ray2.50B1-512[»]
3EGWX-ray1.90B1-509[»]
3IR5X-ray2.30B1-512[»]
3IR6X-ray2.80B1-512[»]
3IR7X-ray2.50B1-512[»]
ProteinModelPortalP11349.
SMRP11349. Positions 1-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10312N.
IntActP11349. 13 interactions.
MINTMINT-1260007.
STRING511145.b1225.

Protein family/group databases

TCDB5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbP11349.
PRIDEP11349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74309; AAC74309; b1225.
BAA36095; BAA36095; BAA36095.
GeneID12933237.
945780.
KEGGecj:Y75_p1200.
eco:b1225.
PATRIC32117710. VBIEscCol129921_1277.

Organism-specific databases

EchoBASEEB0633.
EcoGeneEG10639. narH.

Phylogenomic databases

eggNOGCOG1140.
HOGENOMHOG000237353.
KOK00371.
OMAQSPIYKM.
OrthoDBEOG6X3W4C.
PhylomeDBP11349.
ProtClustDBCLSK868287.

Enzyme and pathway databases

BioCycEcoCyc:NARH-MONOMER.
ECOL316407:JW1216-MONOMER.
MetaCyc:NARH-MONOMER.

Gene expression databases

GenevestigatorP11349.

Family and domain databases

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

Other

EvolutionaryTraceP11349.
PROP11349.

Entry information

Entry nameNARH_ECOLI
AccessionPrimary (citable) accession number: P11349
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 146 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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