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Protein

Respiratory nitrate reductase 2 gamma chain

Gene

narV

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 (By similarity).By similarity

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

hemeBy similarityNote: 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Iron (heme B 1 axial ligand)By similarity1
Metal bindingi67Iron (heme B 2 axial ligand)By similarity1
Metal bindingi188Iron (heme B 2 axial ligand)By similarity1
Metal bindingi206Iron (heme B 1 axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

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

BioCyciECOO157:NARV-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 2 gamma chain (EC:1.7.99.4)
Gene namesi
Name:narV
Ordered Locus Names:Z2247, ECs2068
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4PeriplasmicBy similarity4
Transmembranei5 – 30Helical; Name=1By similarityAdd BLAST26
Topological domaini31 – 48CytoplasmicBy similarityAdd BLAST18
Transmembranei49 – 71Helical; Name=2By similarityAdd BLAST23
Topological domaini72 – 83PeriplasmicBy similarityAdd BLAST12
Transmembranei84 – 113Helical; Name=3By similarityAdd BLAST30
Topological domaini114 – 125CytoplasmicBy similarityAdd BLAST12
Transmembranei126 – 149Helical; Name=4By similarityAdd BLAST24
Topological domaini150 – 183PeriplasmicBy similarityAdd BLAST34
Transmembranei184 – 199Helical; Name=5By similarityAdd BLAST16
Topological domaini200 – 226CytoplasmicBy similarityAdd BLAST27

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967321 – 226Respiratory nitrate reductase 2 gamma chainAdd BLAST226

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi155864.Z2247.

Structurei

3D structure databases

ProteinModelPortaliP0AF33.
SMRiP0AF33.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D0D. Bacteria.
COG2181. LUCA.
HOGENOMiHOG000237376.
KOiK00374.
OMAiVLFHVGV.

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.

P0AF33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQYLNVFFY DIYPYICATV FFLGSWLRYD YGQYTWRASS SQMLDKRGMV
60 70 80 90 100
IWSNLFHIGI LGIFFGHLFG MLTPHWMYAW FLPVAAKQLM AMVLGGICGV
110 120 130 140 150
LTLIGGAGLL WRRLTNQRVR ATSTTPDIII MSILLIQCLL GLSTIPFSAQ
160 170 180 190 200
YPDGSEMMKL VGWAQSIVTF RGGSSEMLNG VAFVFRLHLV LGMTIFLLFP
210 220
FTRLVHVWSA PFEYFTRRYQ IVRSRR
Length:226
Mass (Da):26,018
Last modified:December 20, 2005 - v1
Checksum:i1D5FAC307F3D5B84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56305.1.
BA000007 Genomic DNA. Translation: BAB35491.1.
PIRiD90887.
E85730.
RefSeqiNP_310095.1. NC_002695.1.
WP_000617115.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG56305; AAG56305; Z2247.
BAB35491; BAB35491; BAB35491.
GeneIDi917268.
KEGGiece:Z2247.
ecs:ECs2068.
PATRICi18353209. VBIEscCol44059_1824.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56305.1.
BA000007 Genomic DNA. Translation: BAB35491.1.
PIRiD90887.
E85730.
RefSeqiNP_310095.1. NC_002695.1.
WP_000617115.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliP0AF33.
SMRiP0AF33.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z2247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG56305; AAG56305; Z2247.
BAB35491; BAB35491; BAB35491.
GeneIDi917268.
KEGGiece:Z2247.
ecs:ECs2068.
PATRICi18353209. VBIEscCol44059_1824.

Phylogenomic databases

eggNOGiENOG4105D0D. Bacteria.
COG2181. LUCA.
HOGENOMiHOG000237376.
KOiK00374.
OMAiVLFHVGV.

Enzyme and pathway databases

BioCyciECOO157:NARV-MONOMER.

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 nameiNARV_ECO57
AccessioniPrimary (citable) accession number: P0AF33
Secondary accession number(s): P19316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 73 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

Complete proteome

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.