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Protein

Respiratory nitrate reductase 1 gamma chain

Gene

narI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The nitrate reductase enzyme complex 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 activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

hemeNote: Binds 2 heme groups per subunit. Heme 1, called the proximal or heme Bp in PubMed:12910261, is located at the cytoplasmic interface, heme 2, called the distal or heme Bd, is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi56 – 561Iron (heme B 1 axial ligand)
Metal bindingi66 – 661Iron (heme B 2 axial ligand)
Metal bindingi187 – 1871Iron (heme B 2 axial ligand)
Metal bindingi205 – 2051Iron (heme B 1 axial ligand)

GO - Molecular functioni

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • cytochrome complex assembly Source: EcoCyc
  • nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:NARI-MONOMER.
ECOL316407:JW1218-MONOMER.
MetaCyc:NARI-MONOMER.
BRENDAi1.7.5.1. 2026.

Protein family/group databases

TCDBi5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 1 gamma chain (EC:1.7.99.4)
Alternative name(s):
Cytochrome B-NR
Nitrate reductase A subunit gamma
Quinol-nitrate oxidoreductase subunit gamma
Gene namesi
Name:narI
Synonyms:chlI
Ordered Locus Names:b1227, JW1218
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10640. narI.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33Periplasmic1 Publication
Transmembranei4 – 2926Helical; Name=1Add
BLAST
Topological domaini30 – 4718Cytoplasmic1 PublicationAdd
BLAST
Transmembranei48 – 7023Helical; Name=2Add
BLAST
Topological domaini71 – 8212Periplasmic1 PublicationAdd
BLAST
Transmembranei83 – 11230Helical; Name=3Add
BLAST
Topological domaini113 – 12412Cytoplasmic1 PublicationAdd
BLAST
Transmembranei125 – 14824Helical; Name=4Add
BLAST
Topological domaini149 – 18234Periplasmic1 PublicationAdd
BLAST
Transmembranei183 – 19816Helical; Name=5Add
BLAST
Topological domaini199 – 22527Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of membrane Source: EcoCyc
  • nitrate reductase complex Source: CACAO
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Respiratory nitrate reductase 1 gamma chainPRO_0000096723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionine1 Publication

Keywords - PTMi

Formylation

Expressioni

Inductioni

By nitrate.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

DIPiDIP-10313N.
IntActiP11350. 2 interactions.
MINTiMINT-1262739.
STRINGi511145.b1227.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 109Combined sources
Helixi12 – 3019Combined sources
Helixi32 – 343Combined sources
Turni41 – 433Combined sources
Helixi48 – 7124Combined sources
Turni74 – 807Combined sources
Helixi83 – 11432Combined sources
Helixi116 – 1216Combined sources
Helixi124 – 14724Combined sources
Helixi148 – 1503Combined sources
Turni151 – 1533Combined sources
Helixi154 – 16714Combined sources
Helixi173 – 1775Combined sources
Helixi182 – 19716Combined sources
Helixi198 – 2003Combined sources
Helixi202 – 2087Combined sources
Helixi211 – 2155Combined sources
Beta strandi218 – 2225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90C1-225[»]
1SIWX-ray2.20C1-225[»]
1Y4ZX-ray2.00C1-225[»]
1Y5IX-ray1.90C1-225[»]
1Y5LX-ray2.50C1-225[»]
1Y5NX-ray2.50C1-225[»]
3EGWX-ray1.90C1-225[»]
3IR5X-ray2.30C1-225[»]
3IR6X-ray2.80C1-225[»]
3IR7X-ray2.50C1-225[»]
ProteinModelPortaliP11350.
SMRiP11350. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11350.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2181.
HOGENOMiHOG000237376.
InParanoidiP11350.
KOiK00374.
OMAiFPFCRLV.
OrthoDBiEOG6K13W6.
PhylomeDBiP11350.

Family and domain databases

InterProiIPR023234. NarG-like_domain.
IPR003816. Nitrate_red_gam.
[Graphical view]
PfamiPF02665. Nitrate_red_gam. 1 hit.
[Graphical view]
SUPFAMiSSF103501. SSF103501. 1 hit.
TIGRFAMsiTIGR00351. narI. 1 hit.

Sequencei

Sequence statusi: Complete.

P11350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFLNMFFFD IYPYIAGAVF LIGSWLRYDY GQYTWRAASS QMLDRKGMNL
60 70 80 90 100
ASNLFHIGIL GIFVGHFFGM LTPHWMYEAW LPIEVKQKMA MFAGGASGVL
110 120 130 140 150
CLIGGVLLLK RRLFSPRVRA TTTGADILIL SLLVIQCALG LLTIPFSAQH
160 170 180 190 200
MDGSEMMKLV GWAQSVVTFH GGASQHLDGV AFIFRLHLVL GMTLFLLFPF
210 220
SRLIHIWSVP VEYLTRKYQL VRARH
Length:225
Mass (Da):25,497
Last modified:July 1, 1989 - v1
Checksum:iA0D7989D00D05B72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20147 Genomic DNA. Translation: AAA24197.1.
U00096 Genomic DNA. Translation: AAC74311.1.
AP009048 Genomic DNA. Translation: BAA36097.1.
PIRiC27737. RDECNG.
RefSeqiNP_415745.1. NC_000913.3.
WP_001160108.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC74311; AAC74311; b1227.
BAA36097; BAA36097; BAA36097.
GeneIDi945808.
KEGGieco:b1227.
PATRICi32117714. VBIEscCol129921_1279.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20147 Genomic DNA. Translation: AAA24197.1.
U00096 Genomic DNA. Translation: AAC74311.1.
AP009048 Genomic DNA. Translation: BAA36097.1.
PIRiC27737. RDECNG.
RefSeqiNP_415745.1. NC_000913.3.
WP_001160108.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90C1-225[»]
1SIWX-ray2.20C1-225[»]
1Y4ZX-ray2.00C1-225[»]
1Y5IX-ray1.90C1-225[»]
1Y5LX-ray2.50C1-225[»]
1Y5NX-ray2.50C1-225[»]
3EGWX-ray1.90C1-225[»]
3IR5X-ray2.30C1-225[»]
3IR6X-ray2.80C1-225[»]
3IR7X-ray2.50C1-225[»]
ProteinModelPortaliP11350.
SMRiP11350. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10313N.
IntActiP11350. 2 interactions.
MINTiMINT-1262739.
STRINGi511145.b1227.

Protein family/group databases

TCDBi5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74311; AAC74311; b1227.
BAA36097; BAA36097; BAA36097.
GeneIDi945808.
KEGGieco:b1227.
PATRICi32117714. VBIEscCol129921_1279.

Organism-specific databases

EchoBASEiEB0634.
EcoGeneiEG10640. narI.

Phylogenomic databases

eggNOGiCOG2181.
HOGENOMiHOG000237376.
InParanoidiP11350.
KOiK00374.
OMAiFPFCRLV.
OrthoDBiEOG6K13W6.
PhylomeDBiP11350.

Enzyme and pathway databases

BioCyciEcoCyc:NARI-MONOMER.
ECOL316407:JW1218-MONOMER.
MetaCyc:NARI-MONOMER.
BRENDAi1.7.5.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP11350.
PROiP11350.

Family and domain databases

InterProiIPR023234. NarG-like_domain.
IPR003816. Nitrate_red_gam.
[Graphical view]
PfamiPF02665. Nitrate_red_gam. 1 hit.
[Graphical view]
SUPFAMiSSF103501. SSF103501. 1 hit.
TIGRFAMsiTIGR00351. narI. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. "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 1-9, FORMYLATION AT MET-1.
  6. "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.
  7. "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), METAL BINDING AT HIS-56; HIS-66; HIS-187 AND HIS-205.

Entry informationi

Entry nameiNARI_ECOLI
AccessioniPrimary (citable) accession number: P11350
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 22, 2015
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.