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Protein

Anaerobic nitric oxide reductase flavorubredoxin

Gene

norV

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

Functioni

Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.

Cofactori

Protein has several cofactor binding sites:
  • Fe cationNote: Binds 3 Fe cations per monomer.
  • FMNNote: Binds 1 FMN per monomer.

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron 1By similarity
Metal bindingi81 – 811Iron 1By similarity
Metal bindingi83 – 831Iron 2By similarity
Metal bindingi147 – 1471Iron 1By similarity
Metal bindingi166 – 1661Iron 1By similarity
Metal bindingi166 – 1661Iron 2By similarity
Metal bindingi227 – 2271Iron 2By similarity
Metal bindingi428 – 4281Iron 3By similarity
Metal bindingi431 – 4311Iron 3By similarity
Metal bindingi461 – 4611Iron 3By similarity
Metal bindingi464 – 4641Iron 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi260 – 2645FMNBy similarity
Nucleotide bindingi342 – 36928FMNBy similarityAdd
BLAST

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • FMN binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • iron ion binding Source: EcoCyc
  • nitric oxide reductase activity Source: InterPro
  • oxidoreductase activity, acting on other nitrogenous compounds as donors Source: EcoCyc

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7413-MONOMER.
ECOL316407:JW2680-MONOMER.
MetaCyc:G7413-MONOMER.
UniPathwayiUPA00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaerobic nitric oxide reductase flavorubredoxin
Short name:
FlRd
Short name:
FlavoRb
Gene namesi
Name:norV
Synonyms:flrD, ygaI, ygaJ, ygaK
Ordered Locus Names:b2710, JW2680
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12963. norV.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi413 – 47967Missing : Unable to accept electrons from nitric oxide reductase FlrD-NAD(+) reductase (norW). 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Anaerobic nitric oxide reductase flavorubredoxinPRO_0000216785Add
BLAST

Proteomic databases

PaxDbiQ46877.
PRIDEiQ46877.

Expressioni

Inductioni

Submicromolar concentrations of NO induce NorV-dependent NO consumption; as NO reductase is sensitive to oxygen, no activity is detected in its presence. Repressed by oxygen in the presence of NO. Different effects on anaerobic induction in the absence of NO, and in the presence of N(O)3- or N(O)2- have been reported. Transcription is negatively regulated by FNR and does not require NarL or NarP.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

DIPiDIP-28070N.
IntActiQ46877. 10 interactions.
STRINGi511145.b2710.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi9 – 113Combined sources
Beta strandi14 – 185Combined sources
Turni23 – 264Combined sources
Beta strandi33 – 353Combined sources
Beta strandi38 – 4811Combined sources
Helixi53 – 553Combined sources
Helixi56 – 6611Combined sources
Helixi69 – 713Combined sources
Beta strandi74 – 763Combined sources
Turni82 – 843Combined sources
Helixi88 – 947Combined sources
Beta strandi100 – 1023Combined sources
Helixi104 – 11411Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi152 – 1565Combined sources
Turni157 – 1604Combined sources
Beta strandi161 – 1655Combined sources
Turni166 – 1683Combined sources
Helixi179 – 1813Combined sources
Helixi184 – 19815Combined sources
Helixi200 – 2023Combined sources
Helixi203 – 21412Combined sources
Beta strandi221 – 2288Combined sources
Helixi236 – 24611Combined sources
Beta strandi251 – 2588Combined sources
Beta strandi261 – 2633Combined sources
Helixi264 – 27916Combined sources
Beta strandi284 – 2896Combined sources
Helixi290 – 2923Combined sources
Helixi295 – 30410Combined sources
Beta strandi305 – 3117Combined sources
Helixi321 – 33313Combined sources
Beta strandi339 – 34911Combined sources
Helixi352 – 36211Combined sources
Beta strandi371 – 3766Combined sources
Helixi379 – 39618Combined sources
Beta strandi426 – 4283Combined sources
Turni429 – 4313Combined sources
Turni437 – 4393Combined sources
Helixi442 – 4443Combined sources
Turni452 – 4543Combined sources
Turni462 – 4643Combined sources
Beta strandi468 – 4714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MS3NMR-A423-479[»]
4D02X-ray1.76A1-479[»]
ProteinModelPortaliQ46877.
SMRiQ46877. Positions 2-400, 428-474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 393140Flavodoxin-likeAdd
BLAST
Domaini423 – 47452Rubredoxin-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 210181Zinc metallo-hydrolaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family.Curated
Contains 1 flavodoxin-like domain.Curated
Contains 1 rubredoxin-like domain.Curated

Phylogenomic databases

eggNOGiENOG4108ESE. Bacteria.
COG0426. LUCA.
COG1773. LUCA.
HOGENOMiHOG000224529.
InParanoidiQ46877.
KOiK12264.
OMAiGWNGGAV.
OrthoDBiEOG6BGP1J.
PhylomeDBiQ46877.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
HAMAPiMF_01312. NorV.
InterProiIPR023957. Anaer_NO_rdtase_flvorubredoxin.
IPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR001279. Metallo-B-lactamas.
IPR024934. Rubredoxin-like_dom.
IPR016440. Rubredoxin-O_OxRdtase.
IPR004039. Rubredoxin-type_fold.
IPR024935. Rubredoxin_dom.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF00301. Rubredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF005243. ROO. 1 hit.
PRINTSiPR00163. RUBREDOXIN.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56281. SSF56281. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
PS50903. RUBREDOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46877-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIVVKNNIH WVGQRDWEVR DFHGTEYKTL RGSSYNSYLI REEKNVLIDT
60 70 80 90 100
VDHKFSREFV QNLRNEIDLA DIDYIVINHA EEDHAGALTE LMAQIPDTPI
110 120 130 140 150
YCTANAIDSI NGHHHHPEWN FNVVKTGDTL DIGNGKQLIF VETPMLHWPD
160 170 180 190 200
SMMTYLTGDA VLFSNDAFGQ HYCDEHLFND EVDQTELFEQ CQRYYANILT
210 220 230 240 250
PFSRLVTPKI TEILGFNLPV DMIATSHGVV WRDNPTQIVE LYLKWAADYQ
260 270 280 290 300
EDRITIFYDT MSNNTRMMAD AIAQGIAETD PRVAVKIFNV ARSDKNEILT
310 320 330 340 350
NVFRSKGVLV GTSTMNNVMM PKIAGLVEEM TGLRFRNKRA SAFGSHGWSG
360 370 380 390 400
GAVDRLSTRL QDAGFEMSLS LKAKWRPDQD ALKLCREHGR EIARQWALAP
410 420 430 440 450
LPQSTVNTVV KEETSATTTA DLGPRMQCSV CQWIYDPAKG EPMQDVAPGT
460 470
PWSEVPDNFL CPECSLGKDV FEELASEAK
Length:479
Mass (Da):54,234
Last modified:November 1, 1996 - v1
Checksum:i17AC889A6924AB41
GO

Sequence cautioni

The sequence BAA05933.1 differs from that shown. Reason: Frameshift at positions 134 and 411. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28595 Genomic DNA. Translation: BAA05932.1. Frameshift.
D28595 Genomic DNA. Translation: BAA05933.1. Frameshift.
U29579 Genomic DNA. Translation: AAA69220.1.
U00096 Genomic DNA. Translation: AAC75752.1.
AP009048 Genomic DNA. Translation: BAE76787.1.
PIRiB65051.
RefSeqiNP_417190.1. NC_000913.3.
WP_000029634.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75752; AAC75752; b2710.
BAE76787; BAE76787; BAE76787.
GeneIDi948979.
KEGGiecj:JW2680.
eco:b2710.
PATRICi32120818. VBIEscCol129921_2801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28595 Genomic DNA. Translation: BAA05932.1. Frameshift.
D28595 Genomic DNA. Translation: BAA05933.1. Frameshift.
U29579 Genomic DNA. Translation: AAA69220.1.
U00096 Genomic DNA. Translation: AAC75752.1.
AP009048 Genomic DNA. Translation: BAE76787.1.
PIRiB65051.
RefSeqiNP_417190.1. NC_000913.3.
WP_000029634.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MS3NMR-A423-479[»]
4D02X-ray1.76A1-479[»]
ProteinModelPortaliQ46877.
SMRiQ46877. Positions 2-400, 428-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-28070N.
IntActiQ46877. 10 interactions.
STRINGi511145.b2710.

Proteomic databases

PaxDbiQ46877.
PRIDEiQ46877.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75752; AAC75752; b2710.
BAE76787; BAE76787; BAE76787.
GeneIDi948979.
KEGGiecj:JW2680.
eco:b2710.
PATRICi32120818. VBIEscCol129921_2801.

Organism-specific databases

EchoBASEiEB2793.
EcoGeneiEG12963. norV.

Phylogenomic databases

eggNOGiENOG4108ESE. Bacteria.
COG0426. LUCA.
COG1773. LUCA.
HOGENOMiHOG000224529.
InParanoidiQ46877.
KOiK12264.
OMAiGWNGGAV.
OrthoDBiEOG6BGP1J.
PhylomeDBiQ46877.

Enzyme and pathway databases

UniPathwayiUPA00638.
BioCyciEcoCyc:G7413-MONOMER.
ECOL316407:JW2680-MONOMER.
MetaCyc:G7413-MONOMER.

Miscellaneous databases

PROiQ46877.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
HAMAPiMF_01312. NorV.
InterProiIPR023957. Anaer_NO_rdtase_flvorubredoxin.
IPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR001279. Metallo-B-lactamas.
IPR024934. Rubredoxin-like_dom.
IPR016440. Rubredoxin-O_OxRdtase.
IPR004039. Rubredoxin-type_fold.
IPR024935. Rubredoxin_dom.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF00301. Rubredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF005243. ROO. 1 hit.
PRINTSiPR00163. RUBREDOXIN.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56281. SSF56281. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
PS50903. RUBREDOXIN_LIKE. 1 hit.
[Graphical view]
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. "A family of flavoproteins in the domains Archaea and Bacteria."
    Wasserfallen A., Ragettli S., Jouanneau Y., Leisinger T.
    Eur. J. Biochem. 254:325-332(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "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, MUTAGENESIS.
  6. "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.
  7. "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.
  8. "Regulation of the flavorubredoxin nitric oxide reductase gene in Escherichia coli: nitrate repression, nitrite induction, and possible post-transcription control."
    da Costa P.N., Teixeira M., Saraiva L.M.
    FEMS Microbiol. Lett. 218:385-393(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION OF EXPRESSION; NEGATIVE REGULATION BY FNR.
    Strain: K12.
  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 nameiNORV_ECOLI
AccessioniPrimary (citable) accession number: Q46877
Secondary accession number(s): Q2MAB9, Q46708, Q46709
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1996
Last modified: January 20, 2016
This is version 145 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.