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Protein

Nitric oxide reductase FlRd-NAD(+) reductase

Gene

norW

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.

Catalytic activityi

Reduced NO reductase rubredoxin + NAD+ = oxidized NO reductase rubredoxin + NADH.

Cofactori

FADCurated

Pathwayi: nitric oxide reduction

This protein is involved in the pathway nitric oxide reduction, which is part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the pathway nitric oxide reduction and in Nitrogen metabolism.

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc
  • oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor Source: EcoCyc
  • rubredoxin-NAD+ reductase activity Source: EcoCyc

GO - Biological processi

  • cellular response to nitric oxide Source: EcoCyc
  • nitric oxide catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEcoCyc:EG12450-MONOMER.
ECOL316407:JW2681-MONOMER.
UniPathwayiUPA00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide reductase FlRd-NAD(+) reductase (EC:1.18.1.-)
Alternative name(s):
Flavorubredoxin reductase
Short name:
FlRd-reductase
Short name:
FlavoRb reductase
Gene namesi
Name:norW
Synonyms:flrR, ygbD
Ordered Locus Names:b2711, JW2681
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12450. norW.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Nitric oxide reductase FlRd-NAD(+) reductasePRO_0000167662Add
BLAST

Proteomic databases

PaxDbiP37596.
PRIDEiP37596.

Expressioni

Inductioni

Submicromolar concentrations of NO induce anaerobic expression. Repressed by oxygen in the presence of NO.

Interactioni

Protein-protein interaction databases

BioGridi4259424. 14 interactions.
STRINGi511145.b2711.

Structurei

3D structure databases

ProteinModelPortaliP37596.
SMRiP37596. Positions 5-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QZF. Bacteria.
COG1251. LUCA.
HOGENOMiHOG000009393.
InParanoidiP37596.
KOiK12265.
OMAiTWVSDID.
OrthoDBiEOG6QVRCJ.
PhylomeDBiP37596.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_01313. NorW.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR023961. NO_rdtase_NorW.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.

Sequencei

Sequence statusi: Complete.

P37596-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNGIVIIGS GFAARQLVKN IRKQDATIPL TLIAADSMDE YNKPDLSHVI
60 70 80 90 100
SQGQRADDLT RQTAGEFAEQ FNLHLFPQTW VTDIDAEARV VKSQNNQWQY
110 120 130 140 150
DKLVLATGAS AFVPPVPGRE LMLTLNSQQE YRACETQLRD ARRVLIVGGG
160 170 180 190 200
LIGSELAMDF CRAGKAVTLI DNAASILASL MPPEVSSRLQ HRLTEMGVHL
210 220 230 240 250
LLKSQLQGLE KTDSGIQATL DRQRNIEVDA VIAATGLRPE TALARRAGLT
260 270 280 290 300
INRGVCVDSY LQTSNTDIYA LGDCAEINGQ VLPFLQPIQL SAMVLAKNLL
310 320 330 340 350
GNNTPLKLPA MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD
360 370
DADQLRAFVV SEDRMKEAFG LLKTLPM
Length:377
Mass (Da):41,404
Last modified:July 19, 2003 - v3
Checksum:iDDE49A55B99E268B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641S → N (Ref. 1) Curated
Sequence conflicti264 – 2641S → N (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28595 Genomic DNA. Translation: BAA05934.1.
U29579 Genomic DNA. Translation: AAA69221.1.
U00096 Genomic DNA. Translation: AAC75753.1.
AP009048 Genomic DNA. Translation: BAE76788.1.
D14422 Genomic DNA. No translation available.
PIRiC65051.
RefSeqiNP_417191.1. NC_000913.3.
WP_000064752.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75753; AAC75753; b2711.
BAE76788; BAE76788; BAE76788.
GeneIDi947088.
KEGGiecj:JW2681.
eco:b2711.
PATRICi32120820. VBIEscCol129921_2802.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28595 Genomic DNA. Translation: BAA05934.1.
U29579 Genomic DNA. Translation: AAA69221.1.
U00096 Genomic DNA. Translation: AAC75753.1.
AP009048 Genomic DNA. Translation: BAE76788.1.
D14422 Genomic DNA. No translation available.
PIRiC65051.
RefSeqiNP_417191.1. NC_000913.3.
WP_000064752.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37596.
SMRiP37596. Positions 5-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259424. 14 interactions.
STRINGi511145.b2711.

Proteomic databases

PaxDbiP37596.
PRIDEiP37596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75753; AAC75753; b2711.
BAE76788; BAE76788; BAE76788.
GeneIDi947088.
KEGGiecj:JW2681.
eco:b2711.
PATRICi32120820. VBIEscCol129921_2802.

Organism-specific databases

EchoBASEiEB2344.
EcoGeneiEG12450. norW.

Phylogenomic databases

eggNOGiENOG4107QZF. Bacteria.
COG1251. LUCA.
HOGENOMiHOG000009393.
InParanoidiP37596.
KOiK12265.
OMAiTWVSDID.
OrthoDBiEOG6QVRCJ.
PhylomeDBiP37596.

Enzyme and pathway databases

UniPathwayiUPA00638.
BioCyciEcoCyc:EG12450-MONOMER.
ECOL316407:JW2681-MONOMER.

Miscellaneous databases

PROiP37596.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_01313. NorW.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR023961. NO_rdtase_NorW.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and characterization of the downstream region of hydA in Escherichia coli."
    Yano K., Ikebukuro K., Takada Y., Tomiyama M., Karube I.
    Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. Ikebukuro K., Nishio M., Yano K., Tomiyama M., Tamiya E., Karube I.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-377.
    Strain: K12.
  5. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner."
    Gomes C.M., Vicente J.B., Wasserfallen A., Teixeira M.
    Biochemistry 39:16230-16237(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, CHARACTERIZATION.
  7. "Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli."
    Gardner A.M., Helmick R.A., Gardner P.R.
    J. Biol. Chem. 277:8172-8177(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FUNCTION.
    Strain: K12 / AB1157.
  8. "A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin."
    Gomes C.M., Giuffre A., Forte E., Vicente J.B., Saraiva L.M., Brunori M., Teixeira M.
    J. Biol. Chem. 277:25273-25276(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FUNCTION.
  9. "Regulation of the nitric oxide reduction operon (norRVW) in Escherichia coli: role of NorR and sigma 54 in the nitric oxide stress response."
    Gardner A.M., Gessner C.R., Gardner P.R.
    J. Biol. Chem. 278:10081-10086(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION OF EXPRESSION; ANAEROBIC AND NO INDUCED EXPRESSION, REQUIREMENT FOR SIGMA 54.
    Strain: K12 / AB1157.

Entry informationi

Entry nameiNORW_ECOLI
AccessioniPrimary (citable) accession number: P37596
Secondary accession number(s): Q2MAB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 19, 2003
Last modified: January 20, 2016
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.