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Protein

Anaerobic nitric oxide reductase flavorubredoxin

Gene

norV

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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 transfer 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

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Transport
LigandFlavoprotein, FMN, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7413-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

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-557904,EBI-557904

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

DIPiDIP-28070N
IntActiQ46877, 10 interactors
STRINGi316385.ECDH10B_2878

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
Turni215 – 217Combined sources3
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

Phylogenomic databases

eggNOGiENOG4108ESE Bacteria
COG0426 LUCA
COG1773 LUCA
HOGENOMiHOG000224529
InParanoidiQ46877
KOiK12264
OMAiSYGWNGG
PhylomeDBiQ46877

Family and domain databases

CDDicd00730 rubredoxin, 1 hit
Gene3Di3.40.50.360, 1 hit
3.60.15.10, 1 hit
HAMAPiMF_01312 NorV, 1 hit
InterProiView protein in InterPro
IPR023957 Anaer_NO_rdtase_flvorubredoxin
IPR008254 Flavodoxin/NO_synth
IPR029039 Flavoprotein-like_sf
IPR001279 Metallo-B-lactamas
IPR036866 RibonucZ/Hydroxyglut_hydro
IPR024934 Rubredoxin-like_dom
IPR016440 Rubredoxin-O_OxRdtase
IPR024935 Rubredoxin_dom
PfamiView protein in Pfam
PF00258 Flavodoxin_1, 1 hit
PF00753 Lactamase_B, 1 hit
PF00301 Rubredoxin, 1 hit
PIRSFiPIRSF005243 ROO, 1 hit
PRINTSiPR00163 RUBREDOXIN
SMARTiView protein in SMART
SM00849 Lactamase_B, 1 hit
SUPFAMiSSF52218 SSF52218, 1 hit
SSF56281 SSF56281, 1 hit
PROSITEiView protein in PROSITE
PS50902 FLAVODOXIN_LIKE, 1 hit
PS50903 RUBREDOXIN_LIKE, 1 hit

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
PATRICifig|1411691.4.peg.4032

Similar proteinsi

Entry informationi

Entry nameiNORV_ECOLI
AccessioniPrimary (citable) accession number: Q46877
Secondary accession number(s): Q2MAB9, Q46708, Q46709
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 159 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health