Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

heme1 PublicationNote: 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Iron (heme B 1 axial ligand)1 Publication1
Metal bindingi66Iron (heme B 2 axial ligand)1 Publication1
Metal bindingi187Iron (heme B 2 axial ligand)1 Publication1
Metal bindingi205Iron (heme B 1 axial ligand)1 Publication1

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • heme binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • nitrate reductase activity Source: EcoCyc

GO - Biological processi

  • anaerobic electron transport chain Source: GO_Central
  • anaerobic respiration 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10640. narI.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 3Periplasmic1 Publication3
Transmembranei4 – 29Helical; Name=1Add BLAST26
Topological domaini30 – 47Cytoplasmic1 PublicationAdd BLAST18
Transmembranei48 – 70Helical; Name=2Add BLAST23
Topological domaini71 – 82Periplasmic1 PublicationAdd BLAST12
Transmembranei83 – 112Helical; Name=3Add BLAST30
Topological domaini113 – 124Cytoplasmic1 PublicationAdd BLAST12
Transmembranei125 – 148Helical; Name=4Add BLAST24
Topological domaini149 – 182Periplasmic1 PublicationAdd BLAST34
Transmembranei183 – 198Helical; Name=5Add BLAST16
Topological domaini199 – 225Cytoplasmic1 PublicationAdd BLAST27

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • NarGHI complex Source: EcoCyc
  • nitrate reductase complex Source: CACAO
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967231 – 225Respiratory nitrate reductase 1 gamma chainAdd BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1

Keywords - PTMi

Formylation

Proteomic databases

PaxDbiP11350.
PRIDEiP11350.

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.1 Publication

Protein-protein interaction databases

BioGridi4262233. 10 interactors.
DIPiDIP-10313N.
IntActiP11350. 2 interactors.
MINTiMINT-1262739.
STRINGi511145.b1227.

Structurei

Secondary structure

1225
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 10Combined sources9
Helixi12 – 30Combined sources19
Helixi32 – 34Combined sources3
Turni41 – 43Combined sources3
Helixi48 – 71Combined sources24
Turni74 – 80Combined sources7
Helixi83 – 114Combined sources32
Helixi116 – 121Combined sources6
Helixi124 – 147Combined sources24
Helixi148 – 150Combined sources3
Turni151 – 153Combined sources3
Helixi154 – 167Combined sources14
Helixi173 – 177Combined sources5
Helixi182 – 197Combined sources16
Helixi198 – 200Combined sources3
Helixi202 – 208Combined sources7
Helixi211 – 215Combined sources5
Beta strandi218 – 222Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11350.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG41076YT. Bacteria.
COG2181. LUCA.
HOGENOMiHOG000237376.
InParanoidiP11350.
KOiK00374.
OMAiDIMILTL.
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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74311; AAC74311; b1227.
BAA36097; BAA36097; BAA36097.
GeneIDi945808.
KEGGiecj:JW1218.
eco: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_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262233. 10 interactors.
DIPiDIP-10313N.
IntActiP11350. 2 interactors.
MINTiMINT-1262739.
STRINGi511145.b1227.

Protein family/group databases

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

Proteomic databases

PaxDbiP11350.
PRIDEiP11350.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74311; AAC74311; b1227.
BAA36097; BAA36097; BAA36097.
GeneIDi945808.
KEGGiecj:JW1218.
eco:b1227.
PATRICi32117714. VBIEscCol129921_1279.

Organism-specific databases

EchoBASEiEB0634.
EcoGeneiEG10640. narI.

Phylogenomic databases

eggNOGiENOG41076YT. Bacteria.
COG2181. LUCA.
HOGENOMiHOG000237376.
InParanoidiP11350.
KOiK00374.
OMAiDIMILTL.
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...

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: November 2, 2016
This is version 157 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

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 one 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.