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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)DescriptionActionsGraphical viewLength
Metal bindingi79Iron 1By similarity1
Metal bindingi81Iron 1By similarity1
Metal bindingi83Iron 2By similarity1
Metal bindingi147Iron 1By similarity1
Metal bindingi166Iron 1By similarity1
Metal bindingi166Iron 2By similarity1
Metal bindingi227Iron 2By similarity1
Metal bindingi428Iron 3By similarity1
Metal bindingi431Iron 3By similarity1
Metal bindingi461Iron 3By similarity1
Metal bindingi464Iron 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi260 – 264FMNBy similarity5
Nucleotide bindingi342 – 369FMNBy similarityAdd BLAST28

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi413 – 479Missing : Unable to accept electrons from nitric oxide reductase FlrD-NAD(+) reductase (norW). 1 PublicationAdd BLAST67

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002167851 – 479Anaerobic nitric oxide reductase flavorubredoxinAdd BLAST479

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 interactors.
STRINGi511145.b2710.

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi9 – 11Combined sources3
Beta strandi14 – 18Combined sources5
Turni23 – 26Combined sources4
Beta strandi33 – 35Combined sources3
Beta strandi38 – 48Combined sources11
Helixi53 – 55Combined sources3
Helixi56 – 66Combined sources11
Helixi69 – 71Combined sources3
Beta strandi74 – 76Combined sources3
Turni82 – 84Combined sources3
Helixi88 – 94Combined sources7
Beta strandi100 – 102Combined sources3
Helixi104 – 114Combined sources11
Beta strandi121 – 123Combined sources3
Beta strandi129 – 133Combined sources5
Beta strandi136 – 142Combined sources7
Beta strandi146 – 148Combined sources3
Beta strandi152 – 156Combined sources5
Turni157 – 160Combined sources4
Beta strandi161 – 165Combined sources5
Turni166 – 168Combined sources3
Helixi179 – 181Combined sources3
Helixi184 – 198Combined sources15
Helixi200 – 202Combined sources3
Helixi203 – 214Combined sources12
Beta strandi221 – 228Combined sources8
Helixi236 – 246Combined sources11
Beta strandi251 – 258Combined sources8
Beta strandi261 – 263Combined sources3
Helixi264 – 279Combined sources16
Beta strandi284 – 289Combined sources6
Helixi290 – 292Combined sources3
Helixi295 – 304Combined sources10
Beta strandi305 – 311Combined sources7
Helixi321 – 333Combined sources13
Beta strandi339 – 349Combined sources11
Helixi352 – 362Combined sources11
Beta strandi371 – 376Combined sources6
Helixi379 – 396Combined sources18
Beta strandi426 – 428Combined sources3
Turni429 – 431Combined sources3
Turni437 – 439Combined sources3
Helixi442 – 444Combined sources3
Turni452 – 454Combined sources3
Turni462 – 464Combined sources3
Beta strandi468 – 471Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MS3NMR-A423-479[»]
4D02X-ray1.76A1-479[»]
5LLDX-ray2.65A1-479[»]
5LMCX-ray1.90A1-479[»]
ProteinModelPortaliQ46877.
SMRiQ46877.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini254 – 393Flavodoxin-likeAdd BLAST140
Domaini423 – 474Rubredoxin-likeAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 210Zinc metallo-hydrolaseAdd BLAST181

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.
PhylomeDBiQ46877.

Family and domain databases

CDDicd00730. rubredoxin. 1 hit.
Gene3Di2.20.28.10. 1 hit.
3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
HAMAPiMF_01312. NorV. 1 hit.
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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MS3NMR-A423-479[»]
4D02X-ray1.76A1-479[»]
5LLDX-ray2.65A1-479[»]
5LMCX-ray1.90A1-479[»]
ProteinModelPortaliQ46877.
SMRiQ46877.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-28070N.
IntActiQ46877. 10 interactors.
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.
PhylomeDBiQ46877.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ46877.

Family and domain databases

CDDicd00730. rubredoxin. 1 hit.
Gene3Di2.20.28.10. 1 hit.
3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
HAMAPiMF_01312. NorV. 1 hit.
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...

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: November 30, 2016
This is version 149 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.